SitesBLAST

C204 (≠ S188) mutation to S: Destabilizes the protein structure; when associated with S-326.
C326 (≠ T317) mutation to S: Destabilizes the protein structure; when associated with S-204.
D419 (= D411) mutation to A: Still allows binding to Mlc.
C421 (= C413) modified: Phosphocysteine; mutation to D: Still allows binding to Mlc. Derepression of Mlc targets becomes constitutive, i.e. independent of PTS phosphorylation.; mutation to S: Unable to be phosphorylated and to catalyze the phosphoryl exchange between glucose and glucose 6-phosphate at equilibrium. Remains susceptible to CdiA toxin from E.coli strain 3006. Still allows binding to Mlc. Derepression of Mlc targets becomes constitutive, i.e. independent of PTS phosphorylation.
I422 (= I414) mutation to A: Still allows binding to Mlc.
T423 (= T415) mutation to A: Decreases Mlc binding.
R424 (= R416) mutation R->A,H: Cannot bind Mlc. Destroys the ability of Cys-421 to be phosphorylated in vitro.; mutation to K: Cannot bind Mlc. Cys-421 can be phosphorylated in vitro.
R426 (= R418) mutation to A: Still allows binding to Mlc. Cys-421 is weakly phosphorylated in vitro.
V449 (= V441) mutation to Q: Interaction with Mlc is hardly detectable.
A451 (≠ S443) mutation to F: The complex with Mlc shows much weaker association than the wild-type.
Q456 (= Q448) mutation to A: Decreases Mlc binding. Interaction with Mlc is hardly detectable.
I458 (= I450) mutation to A: Still allows binding to Mlc.

8qsrA Cryo-em structure of the glucose-specific pts transporter iicb from e. Coli in the inward-facing conformation (see paper)
66% identity, 80% coverage: 2:377/468 of query aligns to 1:383/383 of 8qsrA

query
sites
8qsrA

N

N

I

A

F

F

G

A

S

N

L

L

Q

Q

K

K

V

V

G

G

K

K

S

S

L

L

M

M

L

L

P

P

V

V

S

S

V

V

L

L

P

P

I

I

A

A

G

G

I

I

L

L

G

G

V

V

G

G

A

S

A

A

K

N

F

F

A

S

I

W

L

L

P

P

E

A

V

V

S

S

Q

H

L

V

M

M

E

A

Q

E

A

A

G

G

A

S

V

V

F

F

G

A

N

N

M

M

A

P

L

L

L

I

F

F

A

A

I

I

G

G

V

V

A

A

L

L

G

G

F

F

T

T

K

N

N

N

D

D

G

G

V

V

A

S

G

A

L

L

A

A

A

V

V

V

G

A

Y

Y

Y

G

I

I

M

M

M

V

Q

K

T

T

V

M

E

A

T

V

L

V

A

A

P

P

G

L

-

V

-

L

-

H

-

L

-

P

-

A

-

E

-

I

-

A

-

S

-

K

-

H

-

L

A

A

N

D

T

T

G

G

V

V

L

L

G

G

I

I

A

S

G

G

G

A

I

I

A

A

A

Y

M

M

F

F

N

N

R

R

F

F

Y

Y

N

R

I

I

T

K

L

L

P

P

E

E

Y

Y

L

L

G

G

F

F

A

A

G

G

K

K

R

R

A

F

V

V

P

P

I

I

M

I

T

S

G

G

L

L

S

A

A

A

I

I

V

F

M

T

G

G

A

V

V

V

L

L

A

S

V

F

I

I

W

W

P

P

I

I

G

G

S

S

A

A

I

I

A

Q

A

T

F

F

S

S

D

Q

W

W

A

A

H

Y

Q

Q

N

N

P

P

T

V

V

V

A

A

F

F

G

G

I

I

Y

Y

G

G

V

F

V

I

E

E

R
|
R

S

C

L

L

I

V

P

P

F

F

G

G

L

L

H

H

I

I

W

W

N

N

V

V

P

P

F

F

F

Q

F

M

E

Q

A

I

G

G

S

E

C

Y

T

T

S

N

A

A

S

A

G

G

E

Q

Q

V

L

F

N

H

G

G

I

D

L

I

T

P

C

R

Y

Y

L

M

S

A

A

G

D

D

D

P

A

T

T

A

R

-

A

-

G

-

N

-

G

-

F

-

G

G

Q

K

L

L

A

S

G

G

Y

F

M

L

F

F

K
|
K

M

M

F

Y

G

G

L

L

P

P

A

A

I

I

A

A

I

I

A

W

H

H

S

S

A

A

K

K

P

P

E

E

N

N

R

R

A

A

K

K

V

V

M

G

G

G

I

I

M

M

A

I

S

S

A

A

L

L

T

T

S

S

F

F

L

L

T

T

G

G

I

I

T
|
T

E
|
E

P

P

I

I

E

E

F

F

A

S

F

F

L

M

F

F

V

V

A

A

P

P

V

I

L

L

Y

Y

A

I

I

I

H

H

A

A

L

I

L

L

A

A

G

G

S

L

A

A

F

F

V

P

V

I

T

C

N

I

M

L

L

L

G

G

M

M

V

R

H

D

G

G

T

T

S

S

F
|
F

S

S

H

H

G

G

L

L

I

I

D

D

F

F

L

I

V

V

L

L

S

S

A

G

N

N

A

S

E

S

K

K

M

L

I

W

Y

L

F

F

V

P

V

I

I

V

G

G

L

I

V

G

Y

Y

A

A

A

I

I

V

Y

Y

T

T

L

I

F

F

R

R

I

V

V

L

I

I

K

K

A

A

L

L

D

D

L

L

K

K

T

T

P

P

G

G

R

R

binding beta-D-glucopyranose: R200 (= R187), K254 (= K248), T294 (= T288), E295 (= E289), F334 (= F328)

P09323 PTS system N-acetylglucosamine-specific EIICBA component; EIICBA-Nag; EII-Nag; EC 2.7.1.193 from Escherichia coli (strain K12) (see paper)
40% identity, 100% coverage: 1:468/468 of query aligns to 1:468/648 of P09323

query
sites
P09323

M
|
M

N

N

I

I

F

L

G

G

S

F

L

F

Q

Q

K

R

V

L

G

G

K

R

S

A

L

L

M

Q

L

L

P

P

V

I

S

A

V

V

L

L

P

P

I

V

A

A

G

A

I

L

L

L

G

R

V

F

G

G

A

Q

A

-

K

-

F

-

A

-

I

-

L

-

P

P

E

D

V

L

S

N

-

V

Q

A

L

F

M

I

E

A

Q

Q

A

A

G

G

A

A

V

I

F

F

G

D

N

N

M

L

A

A

L

L

L

I

F

F

A

A

I

I

G

G

V

V

A

A

L

S

G

S

F

W

T

S

K

K

N

D

D

S

G

A

V

G

A

A

G

A

L

A

A

L

A

A

A

G

V

A

G

V

-

G

Y

Y

Y

F

I

V

M

L

M

T

Q

K

T

A

V

M

E

V

T

T

L

I

A

N

P

P

G

E

A

I

N

N

T

M

G

G

V

V

L

L

G

A

G

G

I

I

A

T

G

G

G

L

I

V

A

G

A

A

M

A

F

Y

N

N

R

R

F

W

Y

S

N

D

I

I

T

K

L

L

P

P

E

D

Y

F

L

L

G

S

F

F

A

G

G

G

K

K

R

R

A

F

V

V

P

P

I

I

M

A

T

T

G

G

L

F

S

F

A

C

I

L

V

V

M

L

G

A

A

A

V

I

L

F

A

G

V

Y

I

V

W

W

P

P

I

V

G

Q

S

H

A

A

I

I

A

H

A

A

F

G

S

G

D

E

W

W

A

I

A

V

H

S

Q

A

N

G

P

-

T

A

V

L

A

G

F

S

G

G

I

I

Y

F

G

G

V

F

V

I

E

N

R

R

S

L

L

L

I

I

P

P

F

T

G

G

L

L

H

H

H

Q

I

V

W

L

N

N

V

T

P

I

F

A

F

W

F

F

E

Q

A

I

G

G

S

E

C

F

T

T

S

N

A

A

S

A

G

G

E

T

Q

V

L

F

N

H

G

G

I

D

L

I

T

N

C

R

Y

F

L

Y

S

A

A

G

D

D

D

G

A

T

T

A

R

G

A

M

A

F

G

M

N

S

G

G

F

F

G

-

Q

-

L

-

A

-

G

-

Y

F

M

P

F

I

K

M

M

M

F

F

G

G

L

L

P

P

A

G

A

A

I

L

A

A

I

M

A

Y

H

F

S

A

A

A

K

P

P

K

E

E

N

R

R

R

A

P

K

M

V

V

M

G

G

G

I

M

M

L

A

L

S

S

A

V

A

A

L

V

T

T

S

A

F

F

L

L

T

T

G

G

I

V

T

T

E

E

P

P

I

L

E

E

F

F

A

L

F

F

L

M

F

F

V

L

A

A

P

P

V

L

L

L

Y

Y

A

L

I

L

H

H

A

A

L

L

A

T

G

G

S

I

A

S

F

L

V

F

V

V

T

A

N

T

M

L

L

L

G

G

M

I

V

H

H

A

G

G

T

F

S

S

F

F

S

S

H

A

G

G

L

A

I

I

D

D

F

Y

L

A

V

L

-

M

-

Y

-

N

L

L

S

P

A

A

N

A

A

S

E

Q

K

N

M

V

I

W

Y

M

F

L

V

L

V

V

I

M

G

G

L

V

V

I

Y

F

A

F

A

A

I

I

Y

Y

Y

F

T

V

L

V

F

F

R

S

I

L

V

V

I

I

K

R

A

M

L

F

D

N

L

L

K

K

T

T

P

P

G

G

R

R

E

E

D

D

E

K

E

E

A

D

E

E

-

I

-

V

-

T

E

E

V

A

H

N

V

S

N

N

S

T

S

E

E

E

-

G

-

L

-

T

-

Q

M

L

A

A

I

T

L

N

L

Y

V

I

A

A

F

V

G

G

K

T

A

D

N

N

I

L

E

K

N

A

L

I

D

D

A

A

C

C

I

I

T

T

R

R

L

L

R

R

I

L

S

T

V

V

N

A

D

D

I

S

A

A

L

R

V

V

D

N

K

D

A

T

E

M

L

C

K

K

K

R

L

L

G

G

A

A

A

S

G

G

V

V

-

K

V

L

S

N

G

K

N

Q

G

T

V

I

Q

Q

A

V

I

I

F

V

G

G

T

A

K

K

S

A

D

E

N

S

L

I

K

G

T

D

D

A

M

M

E

K

A

K

Y

V

L

V

A

A

K

R

M1 (= M1) modified: N-formylmethionine

6bvgA Crystal structure of bcmalt t280c-e54c crosslinked by divalent mercury (see paper)
31% identity, 80% coverage: 4:377/468 of query aligns to 2:442/447 of 6bvgA

query
sites
6bvgA

F

F

G

D

S

F

L

W

Q

Q

K

K

V

F

G

G

K

K

S

A

L

L

M

L

L

V

P

V

V

V

S

A

V

V

L

M

P

P

I

A

A

A

G

G

I

L

L

M

L

I

G

S

V

I

G

G

-

K

-

L

-

I

-

G

-

M

A

S

A

A

K

G

F

D

A

I

I

N

L

A

P

V

E

H

V

T

V

I

S

A

Q

R

L

V

M

M

E

C

Q

D

A

I

G

G

G

W

A

A

V

I

F

I

G

T

N

N

M

L

A

H

L

I

L

L

F

F

A

A

I

V

G

A

V

I

A

G

L

G

G

S

F

W

T

A

K

K

N

D

-

R

-

A

-

G

-

A

-

F

-

A

-

L

-

A

-

F

-

V

-

L

-

T

-

N

-

R

-

I

-

T

-

G

-

A

-

I

-

F

-

G

-

V

-

N

-

A

-

E

-

M

-

L

-

A

D

D

G

S

V

K

A

A

G

K

L

V

A

S

A

V

V

L

G

A

Y

G

Y

D

I

L

M

I

M

V

Q

K

T

D

V

Y

E

F

T

T

L

S

-

V

-

L

-

G

A

A

P

P

G

A

A

L

N

N

T

M

G

G

V

V

L

F

G

V

G

G

I

I

A

T

G

G

G

F

I

L

A

G

A

A

A

T

M

L

F

Y

N

N

R

K

F

Y

Y

Y

N

N

I

Y

T

N

-

K

L

L

P

P

E

Q

Y

A

L

L

G

A

F

F

A

N

G

G

K

K

R

R

A

F

V

V

P

P

I

F

M

V

T

V

G

I

L

V

S

W

A

S

I

T

V

V

M

T

G

A

A

I

V

V

L

L

A

S

V

L

I

L

W

W

P

P

P

F

I

I

G

Q

S

S

A

G

I

L

A

N

A

E

F

F

S

G

D

R

W

W

A

I

A

A

H

A

Q

S

N

K

-

D

-

S

-

A

P

P

T

I

V

V

A

A

F

P

G

F

I

V

Y

Y

G

G

V

T

V

L

E
|
E

R
|
R

S

L

L

L

I

L

P

P

F

F

G

G

L

L

H
|
H

I

M

W

L

N
x
T

V

I

P

P

F

M

F

N

F
x
Y

E

T

-

E

-

L

A

G

G

G

S

T

C

Y

T

T

S

M

A

L

S

T

G

G

E

S

Q

K

L

V

N

G

G

Q

I

V

L

V

T

A

-

G

-

Q

-

D

-

P

-

L

-

W

-

L

-

A

-

W

-

I

C

C

Y

D

L

L

S

N

-

N

-

L

A

A

D

N

D

G

A

D

T

T

R

K

A

A

A

Y

G

N

N

D

G

L

F

L

G

N

Q

N

L

V

-

V

-

P

-

A

-

R

-

F

-
x
K

A

A

G

G

G

Q

Y

V

M

I

F

G

K

S

M

T

F

A

G

A

L

L

P

M

A

G

A

I

A

A

I

F

A

A

I

M

A

F

H

R

S

N

A

V

K

D

P

K

E

E

N

K

R

R

A

A

K

K

V

Y

M

K

G

P

I

M

M

F

A

L

S

S

A

A

L

L

T

A

S

V

F

F

L

L

T

T

G

G

I

V

T
|
T

E
|
E

P

P

I

I

E

E

F

F

A

M

F

F

L

M

F

F

V

I

A

A

P

P

V

V

L

L

Y

Y

A

V

I

V

H

Y

A

A

L

I

L

T

A

T

G

G

S

L

A

A

F

F

V

A

V

L

T

A

N

D

M

L

L

I

G

N

M

L

-

R

V

V

H

H

G

A

T
x
F

S

G

F

F

S

I

H

E

G

-

L

L

I

I

D

T

F

R

L

T

V

P

L

M

S

M

A

V

N

N

A

A

-

G

-

L

-

T

E

R

K

D

M

L

I

I

Y

N

F

F

V

V

V

I

I

V

G

S

L

L

V

V

Y

F

A

F

A

G

I

L

Y

N

Y

F

T

T

L

L

F

F

R

N

I

F

V

L

I

I

K

K

A

K

L

F

D

N

L

L

K

P

T

T

P

P

G

G

R

R

binding alpha-D-glucopyranose: E227 (= E186), R228 (= R187), H236 (= H195), H237 (= H196), H237 (= H196), T240 (≠ N199), Y245 (≠ F204), K303 (vs. gap), T350 (= T288), E351 (= E289), F389 (≠ T326)

1o2fB Complex of enzyme iiaglc and iibglc phosphocarrier protein hpr from escherichia coli nmr, restrained regularized mean structure (see paper)
77% identity, 16% coverage: 392:466/468 of query aligns to 1:75/77 of 1o2fB

query
sites
1o2fB

E

E

M

M

A

A

I

A

L

A

L

L

V

V

A

A

F

F

G

G

K

K

A

E

N

N

I

I

E

T

N

N

L

L

D

D

A

A

C
|
C

I
|
I

T
|
T

R

R

L

L

R

R

I

V

S

S

V

V

N

A

D

D

I

V

A

S

L

K

V

V

D

D

K

Q

A

A

E

G

L

L

K

K

L

L

G

G

A

A

G

G

V

V

S

A

G

G

N

S

G

G

V

V

Q

Q

A

A

I

I

F

F

G

G

T

T

K

K

S

S

D

D

N

N

L

L

K

K

T

T

D

E

M

M

E

D

A

E

Y

Y

L

I

binding phosphite ion: C22 (= C413), I23 (= I414), T24 (= T415)

Query Sequence

>WP_019613932.1 NCBI__GCF_000381745.1:WP_019613932.1
MNIFGSLQKVGKSLMLPVSVLPIAGILLGVGAAKFAILPEVVSQLMEQAGGAVFGNMALL
FAIGVALGFTKNDGVAGLAAAVGYYIMMQTVETLAPGANTGVLGGIIAGGIAAAMFNRFY
NITLPEYLGFFAGKRAVPIMTGLSAIVMGAVLAVIWPPIGSAIAAFSDWAAHQNPTVAFG
IYGVVERSLIPFGLHHIWNVPFFFEAGSCTSASGEQLNGILTCYLSADDATRAAGNGFGQ
LAGGYMFKMFGLPAAAIAIAHSAKPENRAKVMGIMASAALTSFLTGITEPIEFAFLFVAP
VLYAIHALLAGSAFVVTNMLGMVHGTSFSHGLIDFLVLSANAEKMIYFVVIGLVYAAIYY
TLFRIVIKALDLKTPGREDEEAEEEVHVNSSEMAILLVAAFGGKANIENLDACITRLRIS
VNDIALVDKAELKKLGAAGVVVSGNGVQAIFGTKSDNLKTDMEAYLAK

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