SitesBLAST

Q980R9 N-alpha-acetyltransferase; NAT; Amino-terminal acetyltransferase; N-terminal acetyltransferase; EC 2.3.1.255; EC 2.3.1.258 from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see 4 papers)
29% identity, 98% coverage: 3:160/162 of query aligns to 11:165/167 of Q980R9

query
sites
Q980R9

E

D

I

F

V

T

I

L

R

R

H

N

A

A

E

R

T

M

R

D

D

D

Y

I

E

D

A

Q

I

I

R

I

Q

K

I

I

H

N

-

R

-

L

A

T

Q
x
L

P
|
P

E
|
E

V

N

Y
|
Y

C

P

N

Y

T

Y

L

F

Q

F

V

V

P

E

H

H

P

L

S

K

D

E

H

Y

M

-

W

-

Q

-

E

-

R

-

L

-

A

-

D

-

R

-

P

-

G

G

I

L

K

A

Q

F

L

F

V

V

A

A

C

I

I

V

D

D

G

N

D

S

V

V

G

G

H

Y

L

I

T

M

-

P

-

R

-

I

-

E

-

W

-

G

-

F

I
x
S

D

N

V

I

Q

K

Q

Q

R

L

P

P

-
x
S

-

L

-

V

R

R

R

K

S

G

H
|
H

V

V

A

V

D

-

F

-

G

S

I
|
I

C
x
A

V
|
V

D

L

S

E

R

E

W

Y

K

R

N
x
R

R
x
K

G
|
G

V
x
I

A
|
A

S
x
T

A

T

L

L

M

L

R

E

E

A

M

S

I

M

E

K

M

S

C

M

D

K

N

N

W

D

L

Y

R

N

V

A

D

E

R

E

I

I

E
x
Y

L

L

T
x
E

V

V

F
x
R

V

V

D

S

N
|
N

A

Y

P

P

A

A

I

I

K

A

V

L

Y
|
Y

K
x
E

K
|
K

Y

L

G

N

F

F

E

K

I

K

E

V

G

K

T

V

G

L

K

K

K

G

Y

Y

A

-

L
x
Y

R

A

N

D

G

G

E

E

Y

-

V

-

D

D

A

A

Y

Y

Y

L

M

M

A

A

R

R

L33 (≠ Q23) mutation to A: 20- and 2-fold decrease of the catalytic efficiency and affinity for Ser-N-terminal peptide. 11-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but almost same affinity compared to the wild-type.
P34 (= P24) mutation to A: 20-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. 18-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but almost same affinity compared to the wild-type.
E35 (= E25) Plays an important role in substrate specificity; mutation to A: Slight increase of the catalytic efficiency for Ser-N-terminal peptide, but 4-fold decrease of the affinity compared to the wild-type. 6-fold increase of the catalytic efficiency for Met-N-terminal peptide and slight decrease of the affinity compared to the wild-type.; mutation to F: Strong decrease of the acetyltransferase activity with Ser-N-terminal peptide such as Alba. 2-fold increase of acetyltransferase activity for Ala-N-terminal peptide such as Hjc compared to the wild-type.; mutation to Q: Loss of acetyltransferase activity for Ser and Met-N-terminal peptide; when associated with Gln-127.; mutation to V: Alters the N-terminal substrate specificity and allows large N-terminal end residue of the substrate to be accommodated in a substrate-binding pocket. 4-fold increase of the acetyltransferase activity with Met-N-terminal peptide such as SSB compared to the wild-type. 2-fold increase of acetyltransferase activity with Ala-N-terminal peptide such as Hjc.; mutation to W: Low acetyltransferase activity with Ala-, Met- and Ser-N-terminal peptide.
Y37 (= Y27) binding ; mutation to A: 34-fold decrease of the catalytic efficiency for Ser-N-terminal peptide and slight decrease of the affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide.; mutation to F: Same catalytic efficiency and slight decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. 3-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Met-N-terminal peptide compared to the wild-type.
S75 (≠ I68) Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability; mutation to A: Has a melting temperature about 3 degrees Celsius lower than that of the wild-type.
S82 (vs. gap) Plays an important role in modulating multiple conformations of loop regions and contributes to protein thermostability; mutation to A: Has a melting temperature about 3 degrees Celsius lower than that of the wild-type.
H88 (= H78) binding ; mutation to A: 2.5- and 1.5-fold decrease of the catalytic efficiency and affinity for Ser-N-terminal peptide compared to the wild-type, respectively. Loss of acetyltransferase activity for Met-N-terminal peptide.; mutation to F: 2.5-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide.; mutation to Q: 2.5-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but 1.5-fold increase of the affinity compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide.
IAV 92:94 (≠ ICV 84:86) binding
R100 (≠ N92) mutation to A: 7-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type.
RKGIAT 100:105 (≠ NRGVAS 92:97) binding
T105 (≠ S97) mutation to A: 3-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type.
Y125 (≠ E117) mutation to A: Same catalytic efficiency and 1.7-fold decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. 1.5- and 2.5-fold decrease of the catalytic efficiency and affinity for Met-N-terminal peptide compared to the wild-type, respectively.
E127 (≠ T119) binding ; mutation to A: Same catalytic efficiency and slight decrease of the affinity for Ser-N-terminal peptide compared to the wild-type. Loss of acetyltransferase activity for Met-N-terminal peptide.; mutation to H: 1.3-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but almost same affinity compared to the wild-type. 1.7-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Met-N-terminal peptide compared to the wild-type.; mutation to Q: 2.3-fold decrease of the catalytic efficiency and 1.3-fold increase of the affinity for Ser-N-terminal peptide compared to the wild-type. 5-fold decrease of the catalytic efficiency and slight decrease of the affinity for Met-N-terminal peptide compared to the wild-type. Loss of acetyltransferase activity for Ser and Met-N-terminal peptide; when associated with Gln-35.
R129 (≠ F121) mutation to A: Slight decrease of the catalytic efficiency and of the affinity for Ser-N-terminal peptide compared to teh wild-type. 2.5-fold increase of the catalytic efficiency and almost the same affinity for Met-N-terminal peptide compared to the wild-type.
N132 (= N124) binding ; mutation to A: 4.5-fold decrease of the affinity, with no significant difference in the catalytic efficiency. Same fold compared to the wild-type.
YEK 139:141 (≠ YKK 131:133) binding
Y154 (≠ L147) binding ; mutation to A: 1.3-fold decrease of the catalytic efficiency for Ser-N-terminal peptide, but same affinity compared to the wild-type. 6.5-fold decrease of the catalytic efficiency for Met-N-terminal peptide, but same affinity compared to the wild-type.; mutation to F: Almost same catalytic efficiency for Ser-N-terminal peptide and slight decrease of the affinity compared to the wild-type. 5-fold decrease of the catalytic efficiency for Met-N-terminal peptide and 1.5-fold decrease of the affinity compared to the wild-type.

4pv6G Crystal structure analysis of ard1 from thermoplasma volcanium (see paper)
35% identity, 67% coverage: 54:161/162 of query aligns to 48:148/154 of 4pv6G

query
sites
4pv6G

L

M

V

V

A

Y

C

T

I

V

D

A

G

G

D

S

V

V

G

G

H

F

L

I

T

-

I

-

D

-

V

V

Q

G

Q

S

R

K

P

Y

R

S

R

R

S

T

H

E

V

A

A

R

D

I

F
x
L

G

L

I
x
F

C

A

V
|
V

D

D

S

E

R

R

W

F

K
x
R

N
x
R

R

M

G
|
G

V

V

A
x
G

S
|
S

A

A

L

L

M

M

R

D

E

A

M

F

I

L

E

S

M

L

C

C

-

R

-

E

D

Q

N

N

W

M

L

L

R

S

V

V

D

-

R

-

I

-

E

R

L

L

T

E

V

V

F

R

V

T

D

D

N

N

A

D

P
x
E

A

A

I

I

K
x
R

V
x
F

Y
|
Y

K

K

Y

Y

G

G

F

F

E

V

I

I

E

T

G

A

T

M

G

L

K

P

K

N

Y

Y

A

-

L

-

R

-

N

Y

G

S

E

D

Y

S

V

S

D

N

A

A

Y

Y

Y

T

M

M

A

W

R

R

V

I

binding acetyl coenzyme *a: L73 (≠ F82), F75 (≠ I84), V77 (= V86), R82 (≠ K91), R83 (≠ N92), G85 (= G94), G87 (≠ A96), S88 (= S97), E116 (≠ P126), R119 (≠ K129), F120 (≠ V130), Y121 (= Y131)

Sites not aligning to the query:

binding acetyl coenzyme *a: 27

4pv6A Crystal structure analysis of ard1 from thermoplasma volcanium (see paper)
35% identity, 67% coverage: 54:161/162 of query aligns to 48:148/154 of 4pv6A

query
sites
4pv6A

L

M

V

V

A

Y

C

T

I

V

D

A

G

G

D

S

V

V

G

G

H

F

L

I

T

-

I

-

D

-

V

V

Q

G

Q

S

R

K

P

Y

R

S

R

R

S

T

H

E

V

A

A

R

D

I

F
x
L

G
x
L

I
x
F

C

A

V
|
V

D

D

S

E

R

R

W

F

K
x
R

N
x
R

R

M

G
|
G

V

V

A
x
G

S
|
S

A

A

L

L

M

M

R

D

E

A

M

F

I

L

E

S

M

L

C

C

-

R

-

E

D

Q

N

N

W

M

L

L

R

S

V

V

D

-

R

-

I

-

E

R

L

L

T

E

V

V

F

R

V

T

D

D

N
|
N

A

D

P
x
E

A

A

I

I

K

R

V
x
F

Y
|
Y

K

K

Y

Y

G

G

F

F

E

V

I

I

E

T

G

A

T

M

G

L

K

P

K

N

Y

Y

A

-

L

-

R

-

N

Y

G

S

E

D

Y

S

V

S

D

N

A

A

Y

Y

Y

T

M

M

A

W

R

R

V

I

binding coenzyme a: L73 (≠ F82), L74 (≠ G83), F75 (≠ I84), V77 (= V86), R82 (≠ K91), R83 (≠ N92), G85 (= G94), G87 (≠ A96), S88 (= S97), N114 (= N124), E116 (≠ P126), F120 (≠ V130), Y121 (= Y131)

6d72B Crystal structure of spermidine/spermine n-acetyltransferase speg from yersinia pestis in complex with calcium ions.
37% identity, 45% coverage: 80:152/162 of query aligns to 85:157/176 of 6d72B

query
sites
6d72B

A

A

D

E

F

F

G

Q

I

I

C

I

V

I

D

D

S

P

R

T

W

H

K

Q

N

G

R

K

G

G

V

Y

A

A

S

G

A

A

L

A

M

A

R

K

E

L

M

A

I

M

E

E

M

Y

C

G

D

F

N

S

W

V

L

L

R

N

V

L

D

Y

R

K

I

L

E

Y

L

L

T

I

V

V

F

D

V

K

D

E

N

N

A

E

P

K

A

A

I

I

K

H

V

I

Y

Y

K

S

K

K

Y

L

G

G

F

F

E

E

I

I

E

E

G

G

T

E

G

L

K

K

K

Q

Y

E

A

F

L

F

R

I

N

N

G

G

E

E

Y

Y

Sites not aligning to the query:

binding calcium ion: 36, 77

3ld2B The crystal structure of smu.2055 from streptococcus mutans ua159
30% identity, 62% coverage: 54:154/162 of query aligns to 51:150/162 of 3ld2B

query
sites
3ld2B

L

L

V

V

A

A

C

K

I

I

D

K

G

D

D

K

V

I

V

V

G

G

H

V

L

L

T

D

I

Y

D

S

-

S

V

L

Q

Y

Q

P

R

F

P

P

R

S

R

G

S

Q

H

H

V

I

A

V

D

T

F

F

G

G

I
|
I

C

A

V
|
V

D

A

S

E

R

K

W

E

K
x
R

N
x
R

R

K

G
|
G

V

I

A
x
G

S

-

A

-

L

-

M

-

R
|
R

E

A

M

L

I

V

E

Q

M

I

C

F

D

L

N

N

W

E

L

V

R

K

V

S

D

D

-

Y

-

Q

R

K

I

V

E

L

L

I

T

H

V

V

F

L

V

S

D

S

N

N

A

Q

P
x
E

A
|
A

I

V

K
x
L

V
x
F

Y

Y

K

K

K
|
K

Y

L

G

G

F

F

E

D

I

L

E

E

G

A

T

R

G

L

K

T

K

K

Y

Q

A

F

L

F

R

L

N

K

G

G

E

Q

Y

Y

V

V

D

D

binding coenzyme a: I82 (= I84), V84 (= V86), R89 (≠ K91), R90 (≠ N92), G92 (= G94), G94 (≠ A96), R95 (= R101), E122 (≠ P126), A123 (= A127), L125 (≠ K129), F126 (≠ V130), K129 (= K133)

Sites not aligning to the query:

binding coenzyme a: 23

6c37A Mycobacterium smegmatis rimj in complex with coa-disulfide
34% identity, 63% coverage: 58:159/162 of query aligns to 86:186/209 of 6c37A

query
sites
6c37A

I

L

D

D

G

G

D

E

V

F

V

V

G

G

H

Q

L

L

T

T

I

I

-

G

D

N

V

V

Q

T

Q

H

R

G

P

A

R

L

R

R

S

S

H

-

V

-

A

A

D

W

F

I

G
|
G

I
x
Y

C
x
W

V
|
V

D

A

S

S

R

S

W

R

K
x
T

N
x
G

R

G

G
|
G

V

I

A
|
A

S
x
T

A

A

L

A

M

L

R

A

E

M

M

G

I

L

E

D

M

H

C

C

D

F

N

T

W

A

L

V

R

Q

V

L

D

H

R

R

I

I

E

E

L

A

T
|
T

V

V

F

R

V

P

D

E

N
|
N

A
x
T

P
|
P

A
x
S

I

R

K

A

V
|
V

Y

L

K

A

K
x
H

Y

V

G

G

F

F

E

R

I

E

E

E

G

G

T

L

G

L

K

K

K

R

Y

Y

A

L

L

E

R

V

N

D

G

G

E

A

Y

W

V

R

D

D

A

H

Y

L

M

V

A

A

binding [[(2~{S},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(3~{R})-4-[[3-[2-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyldisulfanyl]ethylamino]-3-oxidanylidene-propyl]amino]-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-butyl] hydrogen phosphate: G110 (= G83), Y111 (≠ I84), W112 (≠ C85), V113 (= V86), T118 (≠ K91), G119 (≠ N92), G121 (= G94), A123 (= A96), T124 (≠ S97), T146 (= T119), N151 (= N124), T152 (≠ A125), P153 (= P126), S154 (≠ A127), V157 (= V130), H160 (≠ K133)

Sites not aligning to the query:

binding [[(2~{S},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(3~{R})-4-[[3-[2-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyldisulfanyl]ethylamino]-3-oxidanylidene-propyl]amino]-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-butyl] hydrogen phosphate: 42, 205

6c32A Mycobacterium smegmatis rimj with accoa
34% identity, 63% coverage: 58:159/162 of query aligns to 86:186/209 of 6c32A

query
sites
6c32A

I

L

D

D

G

G

D

E

V

F

V

V

G

G

H

Q

L

L

T

T

I

I

-

G

D

N

V

V

Q

T

Q

H

R

G

P

A

R

L

R

R

S

S

H

-

V

-

A

A

D

W

F

I

G
|
G

I
x
Y

C
x
W

V
|
V

D

A

S

S

R

S

W

R

K
x
T

N
x
G

R

G

G
|
G

V

I

A
|
A

S
x
T

A

A

L

A

M

L

R

A

E

M

M

G

I

L

E

D

M

H

C

C

D

F

N

T

W

A

L

V

R

Q

V

L

D

H

R

R

I

I

E

E

L

A

T
|
T

V

V

F

R

V

P

D

E

N
|
N

A
x
T

P
|
P

A
x
S

I

R

K

A

V
|
V

Y

L

K

A

K
x
H

Y

V

G

G

F

F

E

R

I

E

E

E

G

G

T

L

G

L

K

K

K

R

Y

Y

A

L

L

E

R

V

N

D

G

G

E

A

Y

W

V

R

D

D

A

H

Y

L

M

V

A

A

binding acetyl coenzyme *a: G110 (= G83), Y111 (≠ I84), W112 (≠ C85), V113 (= V86), T118 (≠ K91), G119 (≠ N92), G121 (= G94), A123 (= A96), T124 (≠ S97), T146 (= T119), N151 (= N124), T152 (≠ A125), P153 (= P126), S154 (≠ A127), V157 (= V130), H160 (≠ K133)

Sites not aligning to the query:

binding acetyl coenzyme *a: 205

6wfgA Crystal structure of human naa50 in complex with an inhibitor (compound 3) identified using DNA encoded library technology (see paper)
30% identity, 50% coverage: 68:148/162 of query aligns to 59:137/150 of 6wfgA

query
sites
6wfgA

I

V

D
|
D

V

H

Q

S

Q

Q

R

N

P

Q

R

K

R

R

S

L

H
x
Y

V

I

A
x
M

D

T

F
x
L

G
|
G

I

-

C
|
C

V

L

D

-

S

A

R

P

W

Y

K
x
R

N
x
R

R

L

G
|
G

V

I

A
x
G

S
x
T

A

K

L

M

M

L

R

N

E

H

M

V

I

L

E

N

M

I

C

C

D

E

N

K

W

D

L

G

R

T

V

F

D

D

R

N

I

I

E
x
Y

L

L

T
x
H

V

V

F
x
Q

V

I

D

S

N
|
N

A

E

P
x
S

A

A

I

I

K
x
D

V
x
F

Y

Y

K

R

K
|
K

Y

F

G

G

F

F

E

E

I

I

E

I

G

E

T

T

G

K

K

K

K

N

Y
|
Y

A
x
Y

L

K

R

R

binding coenzyme a: L73 (≠ F82), G74 (= G83), C75 (= C85), R80 (≠ K91), R81 (≠ N92), G83 (= G94), G85 (≠ A96), T86 (≠ S97), N113 (= N124), S115 (≠ P126), D118 (≠ K129), F119 (≠ V130), K122 (= K133)
binding (2S)-N-[(2S)-3-[1-(3-tert-butyl-1-methyl-1H-pyrazole-5-carbonyl)piperidin-4-yl]-1-(methylamino)-1-oxopropan-2-yl]-6-oxopiperidine-2-carboxamide: D60 (= D69), Y69 (≠ H78), M71 (≠ A80), Y106 (≠ E117), H108 (≠ T119), Q110 (≠ F121), Y134 (= Y145), Y135 (≠ A146)

Sites not aligning to the query:

6wfoA Crystal structure of human naa50 in complex with accoa and an inhibitor (compound 4b) identified using DNA encoded library technology (see paper)
30% identity, 50% coverage: 68:148/162 of query aligns to 62:140/153 of 6wfoA

query
sites
6wfoA

I

V

D

D

V

H

Q

S

Q

Q

R

N

P

Q

R

K

R

R

S

L

H
x
Y

V
x
I

A
x
M

D
x
T

F
x
L

G
|
G

I

-

C
|
C

V

L

D

-

S

A

R

P

W

Y

K
x
R

N
x
R

R

L

G
|
G

V

I

A
x
G

S
x
T

A

K

L

M

M

L

R

N

E

H

M

V

I

L

E

N

M

I

C

C

D

E

N

K

W

D

L

G

R

T

V

F

D

D

R

N

I

I

E

Y

L

L

T
x
H

V

V

F

Q

V

I

D

S

N
|
N

A

E

P
x
S

A
|
A

I

I

K

D

V
x
F

Y

Y

K

R

K
|
K

Y

F

G

G

F

F

E

E

I

I

E

I

G

E

T

T

G

K

K

K

K

N

Y
|
Y

A
x
Y

L
x
K

R
|
R

binding acetyl coenzyme *a: I73 (≠ V79), M74 (≠ A80), T75 (≠ D81), L76 (≠ F82), G77 (= G83), C78 (= C85), R83 (≠ K91), R84 (≠ N92), G86 (= G94), G88 (≠ A96), T89 (≠ S97), N116 (= N124), S118 (≠ P126), A119 (= A127), F122 (≠ V130), K125 (= K133)
binding (4S)-1-methyl-N-{(3S,5R)-5-[4-(methylcarbamoyl)-1,3-thiazol-2-yl]-1-[4-(1H-tetrazol-5-yl)benzene-1-carbonyl]pyrrolidin-3-yl}-2,6-dioxohexahydropyrimidine-4-carboxamide: Y72 (≠ H78), M74 (≠ A80), H111 (≠ T119), Y137 (= Y145), Y138 (≠ A146), K139 (≠ L147), R140 (= R148)

Sites not aligning to the query:

6wfkA Crystal structure of human naa50 in complex with coa and an inhibitor (compound 4a) identified using DNA encoded library technology (see paper)
30% identity, 50% coverage: 68:148/162 of query aligns to 62:140/153 of 6wfkA

query
sites
6wfkA

I

V

D

D

V

H

Q

S

Q

Q

R

N

P

Q

R

K

R

R

S

L

H
x
Y

V

I

A
x
M

D

T

F
x
L

G
|
G

I

-

C
|
C

V

L

D

-

S

A

R

P

W

Y

K
x
R

N
x
R

R

L

G
|
G

V

I

A
x
G

S
x
T

A

K

L

M

M

L

R

N

E

H

M

V

I

L

E

N

M

I

C

C

D

E

N

K

W

D

L

G

R

T

V

F

D

D

R

N

I

I

E

Y

L

L

T
x
H

V

V

F
x
Q

V

I

D

S

N
|
N

A

E

P
x
S

A

A

I

I

K

D

V
x
F

Y

Y

K

R

K
|
K

Y

F

G

G

F

F

E

E

I

I

E

I

G

E

T

T

G

K

K

K

K

N

Y
|
Y

A
x
Y

L
x
K

R
|
R

binding coenzyme a: L76 (≠ F82), G77 (= G83), C78 (= C85), R83 (≠ K91), R84 (≠ N92), G86 (= G94), G88 (≠ A96), T89 (≠ S97), N116 (= N124), S118 (≠ P126), F122 (≠ V130), K125 (= K133)
binding (4S)-1-methyl-N-{(3S,5S)-5-[4-(methylcarbamoyl)-1,3-thiazol-2-yl]-1-[4-(1H-tetrazol-5-yl)benzene-1-carbonyl]pyrrolidin-3-yl}-2,6-dioxohexahydropyrimidine-4-carboxamide: Y72 (≠ H78), M74 (≠ A80), H111 (≠ T119), Q113 (≠ F121), Y137 (= Y145), Y138 (≠ A146), K139 (≠ L147), R140 (= R148)

Sites not aligning to the query:

2ob0C Human mak3 homolog in complex with acetyl-coa
30% identity, 50% coverage: 68:148/162 of query aligns to 60:138/166 of 2ob0C

query
sites
2ob0C

I

V

D

D

V

H

Q

S

Q

Q

R

N

P

Q

R

K

R

R

S

L

H

Y

V

I

A

M

D

T

F
x
L

G
|
G

I

-

C

C

V

L

D

-

S

A

R

P

W

Y

K
x
R

N
x
R

R

L

G
|
G

V

I

A
x
G

S
x
T

A

K

L

M

M

L

R

N

E

H

M

V

I

L

E

N

M

I

C

C

D

E

N

K

W

D

L

G

R

T

V

F

D

D

R

N

I

I

E

Y

L

L

T

H

V

V

F

Q

V

I

D

S

N
|
N

A

E

P
x
S

A
|
A

I

I

K
x
D

V
x
F

Y

Y

K

R

K

K

Y

F

G

G

F

F

E

E

I

I

E

I

G

E

T

T

G

K

K

K

K

N

Y

Y

A

Y

L

K

R

R

binding acetyl coenzyme *a: L74 (≠ F82), G75 (= G83), R81 (≠ K91), R82 (≠ N92), G84 (= G94), G86 (≠ A96), T87 (≠ S97), N114 (= N124), S116 (≠ P126), A117 (= A127), D119 (≠ K129), F120 (≠ V130)

Sites not aligning to the query:

binding acetyl coenzyme *a: 24, 25

6wf5A Crystal structure of human naa50 in complex with a truncated cofactor derived inhibitor (compound 2) (see paper)
30% identity, 50% coverage: 68:148/162 of query aligns to 59:137/165 of 6wf5A

query
sites
6wf5A

I

V

D

D

V

H

Q

S

Q

Q

R

N

P

Q

R

K

R

R

S

L

H

Y

V

I

A
x
M

D

T

F
x
L

G
|
G

I

-

C
|
C

V

L

D

-

S

A

R

P

W

Y

K
x
R

N

R

R

L

G

G

V

I

A

G

S

T

A

K

L

M

M

L

R

N

E

H

M

V

I

L

E

N

M

I

C

C

D

E

N

K

W

D

L

G

R

T

V

F

D

D

R

N

I

I

E

Y

L

L

T
x
H

V

V

F

Q

V

I

D

S

N

N

A

E

P

S

A

A

I

I

K

D

V
x
F

Y
|
Y

K

R

K

K

Y

F

G

G

F

F

E

E

I

I

E

I

G

E

T

T

G

K

K

K

K

N

Y
|
Y

A
x
Y

L
x
K

R

R

binding (2R)-2-hydroxy-3,3-dimethyl-N-{3-oxo-3-[(2-sulfanylethyl)amino]propyl}butanamide: L73 (≠ F82), G74 (= G83), C75 (= C85), R80 (≠ K91), F119 (≠ V130), Y120 (= Y131)
binding : M71 (≠ A80), H108 (≠ T119), Y134 (= Y145), Y135 (≠ A146), K136 (≠ L147)

Sites not aligning to the query:

binding : 23, 25, 27, 31

3tfyA Naa50p amino-terminal acetyltransferase bound to substrate peptide fragment and coa (see paper)
30% identity, 50% coverage: 68:148/162 of query aligns to 63:141/155 of 3tfyA

query
sites
3tfyA

I

V

D

D

V

H

Q

S

Q

Q

R

N

P

Q

R

K

R

R

S

L

H
x
Y

V

I

A
x
M

D

T

F
x
L

G
|
G

I

-

C
|
C

V

L

D

-

S

A

R

P

W

Y

K
x
R

N
x
R

R

L

G
|
G

V

I

A
x
G

S
x
T

A

K

L

M

M

L

R

N

E

H

M

V

I

L

E

N

M

I

C

C

D

E

N

K

W

D

L

G

R

T

V

F

D

D

R

N

I

I

E

Y

L

L

T
x
H

V

V

F

Q

V

I

D

S

N
|
N

A

E

P
x
S

A

A

I

I

K
x
D

V
x
F

Y
|
Y

K

R

K
|
K

Y

F

G

G

F

F

E

E

I

I

E

I

G

E

T

T

G

K

K

K

K

N

Y

Y

A
x
Y

L

K

R

R

binding coenzyme a: L77 (≠ F82), G78 (= G83), C79 (= C85), R84 (≠ K91), R85 (≠ N92), G87 (= G94), G89 (≠ A96), T90 (≠ S97), N117 (= N124), S119 (≠ P126), D122 (≠ K129), F123 (≠ V130), Y124 (= Y131), K126 (= K133)
binding : Y73 (≠ H78), M75 (≠ A80), H112 (≠ T119), Y139 (≠ A146)

Sites not aligning to the query:

binding coenzyme a: 27
binding : 28, 31

Query Sequence

>17502 FitnessBrowser__Keio:17502
MSEIVIRHAETRDYEAIRQIHAQPEVYCNTLQVPHPSDHMWQERLADRPGIKQLVACIDG
DVVGHLTIDVQQRPRRSHVADFGICVDSRWKNRGVASALMREMIEMCDNWLRVDRIELTV
FVDNAPAIKVYKKYGFEIEGTGKKYALRNGEYVDAYYMARVK

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