SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing BWI76_RS13025 FitnessBrowser__Koxy:BWI76_RS13025 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

4ij6A Crystal structure of a novel-type phosphoserine phosphatase mutant (h9a) from hydrogenobacter thermophilus tk-6 in complex with l-phosphoserine (see paper)
32% identity, 98% coverage: 1:202/206 of query aligns to 2:200/207 of 4ij6A

query
sites
4ij6A

M

V

K

K

L

L

I

I

L

L

V

V

R
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R

H
x
A

A

A

E

E

T

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E

E

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W

N
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active site: R8 (= R7), A9 (≠ H8), N15 (= N14), R58 (= R59), E82 (= E83), H150 (= H152)
binding phosphoserine: R8 (= R7), Q21 (= Q20), R58 (= R59), E82 (= E83), H85 (≠ F86), H150 (= H152), T151 (≠ G153)

1h2fA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with trivanadate (see paper)
28% identity, 91% coverage: 3:189/206 of query aligns to 4:188/207 of 1h2fA

query
sites
1h2fA

L

L

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Y

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R

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H

A

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active site: R8 (= R7), H9 (= H8), N15 (= N14), R58 (= R59), E82 (= E83), H150 (= H152)
binding phosphate ion: G142 (≠ Q144), E143 (≠ Q145)
binding trivanadate: R8 (= R7), H9 (= H8), N15 (= N14), Q21 (= Q20), R58 (= R59), E82 (= E83), H150 (= H152), G151 (= G153), V152 (≠ H154)

Sites not aligning to the query:

binding phosphate ion: 1, 2, 3

1h2eA Bacillus stearothermophilus phoe (previously known as yhfr) in complex with phosphate (see paper)
28% identity, 91% coverage: 3:189/206 of query aligns to 4:188/207 of 1h2eA

query
sites
1h2eA

L

L

I

Y

L

L

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T

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R

H
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H

A

G

E

E

T

T

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W

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N
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active site: R8 (= R7), H9 (= H8), N15 (= N14), R58 (= R59), E82 (= E83), H150 (= H152)
binding phosphate ion: R8 (= R7), H9 (= H8), R58 (= R59), E82 (= E83), H150 (= H152)

6m1xC Crystal structure of phosphoserine phosphatase in complex with 3- phosphoglyceric acid from entamoeba histolytica (see paper)
35% identity, 74% coverage: 2:153/206 of query aligns to 3:147/196 of 6m1xC

query
sites
6m1xC

K

K

L

L

I

I

L

L

V

I

R
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H
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H

A

G

E

E

T

T

E

E

W

W

N

N

L

L

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L

G

G

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Q

G

G

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C

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A

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S

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E

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Y

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Q

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H

G
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G

binding 3-phosphoglyceric acid: R8 (= R7), H9 (= H8), Q21 (= Q20), R57 (= R59), E79 (= E83), H146 (= H152), G147 (= G153)

Q7ZVE3 Fructose-2,6-bisphosphatase TIGAR B; TP53-induced glycolysis and apoptosis regulator B; EC 3.1.3.46 from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
34% identity, 66% coverage: 3:137/206 of query aligns to 6:139/257 of Q7ZVE3

query
sites
Q7ZVE3

L

L

I

T

L

I

V

V

R

R

H
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H

A

G

E

E

T

T

E

Q

W

Y

N

N

L

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K

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Q

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A

A

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K

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N

N

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A

A

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N

A

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L

H11 (= H8) active site, Tele-phosphohistidine intermediate

5zr2C Crystal structure of phosphoserine phosphatase mutant (h9a) from entamoeba histolytica in complex with phosphoserine (see paper)
34% identity, 74% coverage: 2:153/206 of query aligns to 3:147/198 of 5zr2C

query
sites
5zr2C

K

K

L

L

I

I

L

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V

I

R
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H

A

A

G

E

E

T

T

E

E

W

W

N

N

L

L

E

L

G

G

I

K

I

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Q

G
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G

H

C

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D

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L

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N

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G

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E

L

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L

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K

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I

N

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Y

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A

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K

A

F

L

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P

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L

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L

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D

L

L

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C

D

K

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N

S

E

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N

Q

K

Q

T

T

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C

C

I

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V

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S

H
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H

G
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G

binding phosphoserine: R8 (= R7), Q21 (= Q20), G22 (= G21), R57 (= R59), E79 (= E83), H146 (= H152), G147 (= G153)

P36623 Phosphoglycerate mutase; PGAM; BPG-dependent PGAM; MPGM; Phosphoglyceromutase; EC 5.4.2.11 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 65% coverage: 3:136/206 of query aligns to 10:146/211 of P36623

query
sites
P36623

L

L

I

V

L

L

V

T

R

R

H

H

A

G

E

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E

E

W

W

N

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G

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x
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x
Y

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Y

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N

S

T37 (≠ R30) modified: Phosphothreonine
S62 (= S55) modified: Phosphoserine
Y96 (≠ F86) modified: Phosphotyrosine

Sites not aligning to the query:

166 modified: Phosphoserine

Q9HIJ2 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; BPG-dependent PGAM; PGAM; Phosphoglyceromutase; dPGM; EC 5.4.2.11 from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) (see paper)
30% identity, 53% coverage: 1:109/206 of query aligns to 1:102/200 of Q9HIJ2

query
sites
Q9HIJ2

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H9 (= H8) mutation to A: Loss of activity.

4pzaB The complex structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c with inorganic phosphate (see paper)
25% identity, 74% coverage: 2:153/206 of query aligns to 4:159/217 of 4pzaB

query
sites
4pzaB

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active site: H10 (= H8), R59 (= R59), E83 (= E83)
binding phosphate ion: R9 (= R7), H10 (= H8), R59 (= R59), E83 (= E83), H158 (= H152), G159 (= G153)

4qihA The structure of mycobacterial glucosyl-3-phosphoglycerate phosphatase rv2419c complexes with vo3 (see paper)
25% identity, 74% coverage: 2:153/206 of query aligns to 3:158/209 of 4qihA

query
sites
4qihA

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active site: H9 (= H8), R58 (= R59), E82 (= E83)
binding vanadate ion: R8 (= R7), H9 (= H8), Q21 (= Q20), R58 (= R59), H157 (= H152)

P9WIC7 Glucosyl-3-phosphoglycerate phosphatase; Mannosyl-3-phosphoglycerate phosphatase; EC 3.1.3.85; EC 3.1.3.70 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
25% identity, 74% coverage: 2:153/206 of query aligns to 5:160/223 of P9WIC7

query
sites
P9WIC7

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R10 (= R7) mutation to A: Loss of phosphatase activity.
H11 (= H8) active site, Tele-phosphohistidine intermediate; mutation to A: Almost completely abolished phosphatase activity.
N17 (= N14) mutation to A: About 5% of wild-type phosphatase activity.
K47 (≠ E46) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
R60 (= R59) mutation to A: Loss of phosphatase activity.
H159 (= H152) mutation to A: About 5% of wild-type phosphatase activity.

Sites not aligning to the query:

209 L→E: Disrupts dimerization of the enzyme, which exists as a monomer and has lost its ability to perform dephosphorylation.

5hr5A Bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
29% identity, 83% coverage: 3:172/206 of query aligns to 226:385/424 of 5hr5A

query
sites
5hr5A

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active site: R230 (= R7), H231 (= H8), N237 (= N14), R280 (= R59), E300 (= E83), H365 (= H152)
binding 6-O-phosphono-beta-D-fructofuranose: H231 (= H8), I242 (= I19), G243 (≠ Q20), E300 (= E83), Y311 (≠ L94), R325 (≠ D112), K329 (vs. gap), Y340 (≠ L123), Q366 (≠ G153), R370 (≠ Q157)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 22, 23, 24, 25, 26, 27, 130, 141, 144, 145, 146, 402
binding citrate anion: 49, 52, 76, 103, 104, 171

Q9NQ88 Fructose-2,6-bisphosphatase TIGAR; TP53-induced glycolysis and apoptosis regulator; TP53-induced glycolysis regulatory phosphatase; EC 3.1.3.46 from Homo sapiens (Human) (see 4 papers)
30% identity, 66% coverage: 3:137/206 of query aligns to 6:139/270 of Q9NQ88

query
sites
Q9NQ88

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H11 (= H8) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-102 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-102; A-198 and 258-N--D-261 Del.
E102 (≠ L96) mutation to A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-198. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-198. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-198 and 258-N--D-261 Del.

Sites not aligning to the query:

198 H→A: Abolishes the ability to lower cellular fructose-2,6-bisphosphate levels, to inhibit the glycolytic activity, to reduce levels of ROS, to increase oxygen consumption and to protect toward hypoxic cell death; when associated with A-11 and A-102. Retains the ability to interact and enhance HK2 activity, to localize to the mitochondria, to limit mitochondrial ROS level increase during hypoxia and to rescued partially crypt growth; when associated with A-11 and A-102. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and 258-N--D-261 Del.
258:261 mutation Missing: Inhibits the ability to interact and enhance HK2 activity, to localize to the mitochondria, to protect against the decrease of mitochondrial membrane potential and to limit mitochondrial ROS level increase during hypoxia. Does not abolish the ability to lower cellular fructose-2,6-bisphosphate levels during hypoxia. Loss of the ability to protect against cell death during hypoxia; when associated with A-11; A-102 and A-198.

P26285 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2; 6PF-2-K/Fru-2,6-P2ase 2; PFK/FBPase 2; 6PF-2-K/Fru-2,6-P2ase heart-type isozyme; EC 2.7.1.105; EC 3.1.3.46 from Bos taurus (Bovine) (see paper)
30% identity, 83% coverage: 3:172/206 of query aligns to 253:412/531 of P26285

query
sites
P26285

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M

N

E

L

L

E

E

D

-

T

-

S

-

H

R

Q

Q

Q

G

T

N

I

V

C

L

I

V

V

I

S

S

H

H

G

Q

H

A

V

V

S

M

Q

R

G

C

T

L

L

L

A

A

I

Y

L

F

K

L

E

D

G

K

T

G

V

A

N

D

S

E

F

L

P

P

Sites not aligning to the query:

467 modified: Phosphoserine; by PKA
476 modified: Phosphothreonine; by AMPK and PKC

5htkA Human heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (pfkfb2) (see paper)
28% identity, 83% coverage: 3:172/206 of query aligns to 222:381/425 of 5htkA

query
sites
5htkA

L

I

I

Y

L

L

V

C

R
|
R

H
|
H

A

G

E

E

T

S

E

E

W

F

N
|
N

L

L

E

L

G

G

I

K

I
|
I

Q
x
G

G

G

H

-

S

-

D

D

S

S

S

G

L

L

T

S

C

V

R

R

G

G

L

K

R

Q

E

F

T

A

S

Q

V

A

L

L

L

R

A

K

A

F

F

L

S

E

A

E

S

Q

E

E

Y

I

Q

T

I

D

E

L

R

K

V

V

Y

W

A

T

S

S

P

Q

L

L

G

K

R
|
R

A

T

W

I

Q

Q

M

T

G

A

Q

E

S

S

L

L

A

G

E

V

H

P

F

Y

H

E

C

-

S

-

L

-

T

-

A

Q

E

W

P

K

A

I

L

L

K

N

E
|
E

Q

I

A

D

F

A

G

G

Q

V

F

C

E

E

G

E

M

M

P

T

L
x
Y

E

A

L

E

L

I

R

E

Q

K

K

R

H

Y

P

P

N

E

Y

E

A

F

N

A

A

L

L
x
R

F

D

R

Q

L

E

D
x
K

A

Y

E

L

Y

Y

C

R

P

Y

P

P

G

G

E

E

S

S

L
x
Y

A

Q

H

D

A

L

S

V

Q

Q

R

R

V

L

M

E

R

P

F

V

L

I

Q

M

N

E

L

L

E

E

D

-

T

-

S

-

H

R

Q

Q

Q

G

T

N

I

V

C

L

I

V

V

I

S

S

H
|
H

G
x
Q

H

A

V

V

S

M

Q
x
R

G

C

T

L

L

L

A

A

I

Y

L

F

K

L

E

D

G

K

T

G

V

A

N

D

S

E

F

L

P

P

active site: R226 (= R7), H227 (= H8), N233 (= N14), R276 (= R59), E296 (= E83), H361 (= H152)
binding 6-O-phosphono-beta-D-fructofuranose: H227 (= H8), I238 (= I19), G239 (≠ Q20), E296 (= E83), Y307 (≠ L94), R321 (≠ L108), K325 (≠ D112), Y336 (≠ L123), Q362 (≠ G153), R366 (≠ Q157)

Sites not aligning to the query:

binding adenosine-5'-triphosphate: 17, 18, 19, 20, 21, 22, 140, 144, 145, 146, 397, 398
binding citrate anion: 48, 61, 72, 99, 100, 167

O60825 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2; 6PF-2-K/Fru-2,6-P2ase 2; PFK/FBPase 2; 6PF-2-K/Fru-2,6-P2ase heart-type isozyme; EC 2.7.1.105; EC 3.1.3.46 from Homo sapiens (Human) (see 2 papers)
28% identity, 83% coverage: 3:172/206 of query aligns to 252:411/505 of O60825

query
sites
O60825

L

I

I

Y

L

L

V

C

R

R

H

H

A

G

E

E

T

S

E

E

W

F

N

N

L

L

E

L

G

G

I

K

I

I

Q

G

G

G

H

-

S

-

D

D

S

S

S

G

L

L

T

S

C

V

R

R

G

G

L

K

R

Q

E

F

T

A

S

Q

V

A

L

L

L

R

A

K

A

F

F

L

S

E

A

E

S

Q

E

E

Y

I

Q

T

I

D

E

L

R

K

V

V

Y

W

A

T

S

S

P

Q

L

L

G

K

R

R

A

T

W

I

Q

Q

M

T

G

A

Q

E

S

S

L

L

A

G

E

V

H

P

F

Y

H

E

C

-

S

-

L

-

T

-

A

Q

E

W

P

K

A

I

L

L

K

N

E

E

Q

I

A

D

F

A

G

G

Q

V

F

C

E

E

G

E

M

M

P

T

L

Y

E

A

L

E

L

I

R

E

Q

K

K

R

H

Y

P

P

N

E

Y

E

A

F

N

A

A

L

L

R

F

D

R

Q

L

E

D

K

A

Y

E

L

Y

Y

C

R

P

Y

P

P

G

G

E

E

S

S

L

Y

A

Q

H

D

A

L

S

V

Q

Q

R

R

V

L

M

E

R

P

F

V

L

I

Q

M

N

E

L

L

E

E

D

-

T

-

S

-

H

R

Q

Q

Q

G

T

N

I

V

C

L

I

V

V

I

S

S

H

H

G

Q

H

A

V

V

S

M

Q

R

G

C

T

L

L

L

A

A

I

Y

L

F

K

L

E

D

G

K

T

G

V

A

N

D

S

E

F

L

P

P

Sites not aligning to the query:

466 modified: Phosphoserine; by AMPK; S→E: Constitutively active mutant that cannot be phosphorylated and further activated by AMPK.
468 modified: Phosphothreonine
483 modified: Phosphoserine; by BRAF
486 modified: Phosphoserine
493 modified: Phosphoserine

6ic0A Human pfkfb3 in complex with a n-aryl 6-aminoquinoxaline inhibitor 4 (see paper)
28% identity, 85% coverage: 3:177/206 of query aligns to 231:395/428 of 6ic0A

query
sites
6ic0A

L

I

I

Y

L

L

V

C

R

R

H

H

A

G

E

E

T

N

E

E

W

H

N

N

L

L

E

Q

G

G

I

R

I

I

Q
x
G

G

G

H

-

S

-

D

D

S

S

S

G

L

L

T

S

C

S

R

R

G

G

L

K

R

K

E

F

T

A

S

S

V

A

L

L

L

S

A

K

A

F

F

V

S

E

A

E

S

Q

E

N

Y

L

Q

K

I

D

E

L

R

R

V

V

Y

W

A

T

S

S

P

Q

L

L

G

K

R

S

A

T

W

I

Q

Q

M

T

G

A

Q

E

S

A

L

L

A

R

E

L

H

P

F

Y

H

E

C

-

S

-

L

-

T

-

A

Q

E

W

P

K

A

A

L

L

K

N

E
|
E

Q

I

A

D

F

A

G

G

Q

V

F

C

E

E

G

E

M

L

P

T

L
x
Y

E

E

L

E

L

I

R

R

Q

D

K

T

H

Y

P

P

N

E

Y

-

A

E

N

Y

A

A

L

L

F
x
R

R

E

L

Q

D

D

A
x
K

E

Y

Y

Y

C

Y

P

R

-

Y

P

P

G

T

G

G

E

E

S

S

L
x
Y

A

Q

H

D

A

L

S

V

Q

Q

R

R

V

L

M

E

R

P

F

V

L

I

Q

M

N

E

L

L

E

E

D

-

T

-

S

-

H

R

Q

Q

Q

E

T

N

I

V

C

L

I

V

V

I

S

C

H

H

G
x
Q

H

A

V

V

S

L

Q
x
R

G

C

T

L

L

L

A

A

I

Y

L

F

K

L

E

D

G

K

T

S

V

A

N

E

S

E

F

M

P

P

R

Y

Y

L

A

K

H

C

P

P

binding 6-O-phosphono-beta-D-fructofuranose: G248 (≠ Q20), E305 (= E83), Y316 (≠ L94), R330 (≠ F109), K334 (≠ A113), Y345 (≠ L123), Q371 (≠ G153), R375 (≠ Q157)

Sites not aligning to the query:

binding 3-[[8-(1-methylindol-6-yl)quinoxalin-6-yl]amino]-~{N}-pyrimidin-5-yl-pyridine-4-carboxamide: 28, 29, 32, 33, 135, 137, 146, 149, 197, 200, 224, 226, 404
binding pyrophosphate 2-: 26, 27, 28, 29, 30, 31, 32, 151, 407

5ajzA Human pfkfb3 in complex with an indole inhibitor 5 (see paper)
28% identity, 85% coverage: 3:177/206 of query aligns to 243:407/440 of 5ajzA

query
sites
5ajzA

L

I

I

Y

L

L

V

C

R
|
R

H
|
H

A

G

E

E

T

N

E

E

W

H

N
|
N

L

L

E

Q

G

G

I

R

I

I

Q
x
G

G

G

H

-

S

-

D

D

S

S

S

G

L

L

T

S

C

S

R

R

G

G

L

K

R

K

E

F

T

A

S

S

V

A

L

L

L

S

A

K

A

F

F

V

S

E

A

E

S

Q

E

N

Y

L

Q

K

I

D

E

L

R

R

V

V

Y

W

A

T

S

S

P

Q

L

L

G

K

R
x
S

A

T

W

I

Q

Q

M

T

G

A

Q

E

S

A

L

L

A

R

E

L

H

P

F

Y

H

E

C

-

S

-

L

-

T

-

A

Q

E

W

P

K

A

A

L

L

K

N

E
|
E

Q

I

A

D

F

A

G

G

Q

V

F

C

E

E

G

E

M

L

P

T

L
x
Y

E

E

L

E

L

I

R

R

Q

D

K

T

H

Y

P

P

N

E

Y

-

A

E

N

Y

A

A

L

L

F
x
R

R

E

L

Q

D

D

A
x
K

E

Y

Y

Y

C

Y

P

R

-

Y

P

P

G

T

G

G

E

E

S

S

L
x
Y

A

Q

H

D

A

L

S

V

Q

Q

R

R

V

L

M

E

R

P

F

V

L

I

Q

M

N

E

L

L

E

E

D

-

T

-

S

-

H

R

Q

Q

Q

E

T

N

I

V

C

L

I

V

V

I

S

C

H
|
H

G
x
Q

H

A

V

V

S

L

Q
x
R

G

C

T

L

L

L

A

A

I

Y

L

F

K

L

E

D

G

K

T

S

V

A

N

E

S

E

F

M

P

P

R

Y

Y

L

A

K

H

C

P

P

active site: R247 (= R7), H248 (= H8), N254 (= N14), S297 (≠ R59), E317 (= E83), H382 (= H152)
binding 6-O-phosphono-beta-D-fructofuranose: G260 (≠ Q20), E317 (= E83), Y328 (≠ L94), R342 (≠ F109), K346 (≠ A113), Y357 (≠ L123), Q383 (≠ G153), R387 (≠ Q157)
binding phosphonic acid: R247 (= R7), H248 (= H8), N254 (= N14), H382 (= H152), Q383 (≠ G153)

Sites not aligning to the query:

binding 2-azanyl-N-[4-[(3-cyano-1H-indol-5-yl)oxy]phenyl]ethanamide: 40, 41, 44, 45, 154, 158, 212, 213, 233, 236, 238

6ibyA Human pfkfb3 in complex with a n-aryl 6-aminoquinoxaline inhibitor 6 (see paper)
28% identity, 85% coverage: 3:177/206 of query aligns to 230:394/428 of 6ibyA

query
sites
6ibyA

L

I

I

Y

L

L

V

C

R

R

H

H

A

G

E

E

T

N

E

E

W

H

N

N

L

L

E

Q

G

G

I

R

I

I

Q
x
G

G

G

H

-

S

-

D

D

S

S

S

G

L

L

T

S

C

S

R

R

G

G

L

K

R

K

E

F

T

A

S

S

V

A

L

L

L

S

A

K

A

F

F

V

S

E

A

E

S

Q

E

N

Y

L

Q

K

I

D

E

L

R

R

V

V

Y

W

A

T

S

S

P

Q

L

L

G

K

R

S

A

T

W

I

Q

Q

M

T

G

A

Q

E

S

A

L

L

A

R

E

L

H

P

F

Y

H

E

C

-

S

-

L

-

T

-

A

Q

E

W

P

K

A

A

L

L

K

N

E
|
E

Q

I

A

D

F

A

G

G

Q

V

F

C

E

E

G

E

M

L

P

T

L
x
Y

E

E

L

E

L

I

R

R

Q

D

K

T

H

Y

P

P

N

E

Y

-

A

E

N

Y

A

A

L

L

F
x
R

R

E

L

Q

D

D

A
x
K

E

Y

Y

Y

C

Y

P

R

-

Y

P

P

G

T

G

G

E

E

S

S

L
x
Y

A

Q

H

D

A

L

S

V

Q

Q

R

R

V

L

M

E

R

P

F

V

L

I

Q

M

N

E

L

L

E

E

D

-

T

-

S

-

H

R

Q

Q

Q

E

T

N

I

V

C

L

I

V

V

I

S

C

H

H

G
x
Q

H

A

V

V

S

L

Q
x
R

G

C

T

L

L

L

A

A

I

Y

L

F

K

L

E

D

G

K

T

S

V

A

N

E

S

E

F

M

P

P

R

Y

Y

L

A

K

H

C

P

P

binding 6-O-phosphono-beta-D-fructofuranose: G247 (≠ Q20), E304 (= E83), Y315 (≠ L94), R329 (≠ F109), K333 (≠ A113), Y344 (≠ L123), Q370 (≠ G153), R374 (≠ Q157)

Sites not aligning to the query:

binding 3-[[8-(1-methylindol-6-yl)quinoxalin-6-yl]amino]-~{N}-[(3~{S})-1-methylpyrrolidin-3-yl]pyridine-4-carboxamide: 27, 31, 32, 134, 136, 145, 148, 196, 199, 200, 223
binding pyrophosphate 2-: 25, 26, 27, 28, 29, 30, 31, 150, 406

6etjA Human pfkfb3 in complex with kan0438241 (see paper)
28% identity, 85% coverage: 3:177/206 of query aligns to 236:400/432 of 6etjA

query
sites
6etjA

L

I

I

Y

L

L

V

C

R
|
R

H
|
H

A

G

E

E

T

N

E

E

W

H

N
|
N

L

L

E

Q

G

G

I

R

I
|
I

Q
x
G

G

G

H

-

S

-

D

D

S

S

S

G

L

L

T

S

C

S

R

R

G

G

L

K

R

K

E

F

T

A

S

S

V

A

L

L

L

S

A

K

A

F

F

V

S

E

A

E

S

Q

E

N

Y

L

Q

K

I

D

E

L

R

R

V

V

Y

W

A

T

S

S

P

Q

L

L

G

K

R
x
S

A

T

W

I

Q

Q

M

T

G

A

Q

E

S

A

L

L

A

R

E

L

H

P

F

Y

H

E

C

-

S

-

L

-

T

-

A

Q

E

W

P

K

A

A

L

L

K

N

E
|
E

Q

I

A

D

F

A

G

G

Q

V

F

C

E

E

G

E

M

L

P

T

L
x
Y

E

E

L

E

L

I

R

R

Q

D

K

T

H

Y

P

P

N

E

Y

-

A

E

N

Y

A

A

L

L

F
x
R

R

E

L

Q

D

D

A
x
K

E

Y

Y

Y

C

Y

P

R

-

Y

P

P

G

T

G

G

E

E

S

S

L
x
Y

A

Q

H

D

A

L

S

V

Q

Q

R

R

V

L

M

E

R

P

F

V

L

I

Q

M

N

E

L

L

E

E

D

-

T

-

S

-

H

R

Q

Q

Q

E

T

N

I

V

C

L

I

V

V

I

S

C

H
|
H

G
x
Q

H

A

V

V

S

L

Q
x
R

G

C

T

L

L

L

A

A

I

Y

L

F

K

L

E

D

G

K

T

S

V

A

N

E

S

E

F

M

P

P

R

Y

Y

L

A

K

H

C

P

P

active site: R240 (= R7), H241 (= H8), N247 (= N14), S290 (≠ R59), E310 (= E83), H375 (= H152)
binding 6-O-phosphono-beta-D-fructofuranose: H241 (= H8), I252 (= I19), G253 (≠ Q20), E310 (= E83), Y321 (≠ L94), R335 (≠ F109), K339 (≠ A113), Y350 (≠ L123), Q376 (≠ G153), R380 (≠ Q157)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 32, 33, 34, 35, 36, 37, 151, 154, 155, 156, 205, 412
binding 4-[[3-(5-fluoranyl-2-oxidanyl-phenyl)phenyl]sulfonylamino]-2-oxidanyl-benzoic acid: 58, 59, 62, 75, 83, 86, 113, 114, 115, 120, 181

Query Sequence

>BWI76_RS13025 FitnessBrowser__Koxy:BWI76_RS13025
MKLILVRHAETEWNLEGIIQGHSDSSLTCRGLRETSVLLAAFSASEYQIERVYASPLGRA
WQMGQSLAEHFHCSLTAEPALKEQAFGQFEGMPLELLRQKHPNYANALFRLDAEYCPPGG
ESLAHASQRVMRFLQNLEDTSSHQQTICIVSHGHVSQGTLAILKEGTVNSFPRYAHPHAS
YSVIDLINGKCIGLKWGIATHLRHLN

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory