4RB4
Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016757 | molecular_function | glycosyltransferase activity |
B | 0016757 | molecular_function | glycosyltransferase activity |
C | 0016757 | molecular_function | glycosyltransferase activity |
D | 0016757 | molecular_function | glycosyltransferase activity |
E | 0016757 | molecular_function | glycosyltransferase activity |
F | 0016757 | molecular_function | glycosyltransferase activity |
G | 0016757 | molecular_function | glycosyltransferase activity |
H | 0016757 | molecular_function | glycosyltransferase activity |
I | 0016757 | molecular_function | glycosyltransferase activity |
J | 0016757 | molecular_function | glycosyltransferase activity |
K | 0016757 | molecular_function | glycosyltransferase activity |
L | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE K 501 |
Chain | Residue |
K | CYS339 |
K | CYS342 |
K | CYS358 |
K | CYS370 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE AQH K 502 |
Chain | Residue |
K | GLN224 |
K | SER225 |
K | THR226 |
K | LYS230 |
K | ILE255 |
K | ASP256 |
K | ARG257 |
K | LEU281 |
K | LEU283 |
K | ARG286 |
K | PRO300 |
K | SER301 |
K | GLY302 |
K | TRP305 |
K | GLU326 |
K | THR107 |
K | LEU108 |
K | GLY109 |
K | ALA110 |
K | PHE187 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE L 501 |
Chain | Residue |
L | CYS339 |
L | CYS342 |
L | CYS358 |
L | CYS370 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AQH L 502 |
Chain | Residue |
L | GLY106 |
L | THR107 |
L | LEU108 |
L | GLY109 |
L | PHE187 |
L | GLN224 |
L | SER225 |
L | THR226 |
L | ILE255 |
L | ASP256 |
L | ARG257 |
L | GLY279 |
L | ARG286 |
L | PRO300 |
L | SER301 |
L | GLY302 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE C 501 |
Chain | Residue |
C | CYS339 |
C | CYS342 |
C | CYS358 |
C | CYS370 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO C 502 |
Chain | Residue |
C | ARG189 |
C | GLU201 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AQH C 503 |
Chain | Residue |
C | THR107 |
C | LEU108 |
C | GLY109 |
C | ALA110 |
C | PHE187 |
C | GLN224 |
C | SER225 |
C | THR226 |
C | LYS230 |
C | ARG257 |
C | LEU283 |
C | ARG286 |
C | PRO300 |
C | SER301 |
C | GLY302 |
C | TRP305 |
C | PHE320 |
C | GLU326 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE D 501 |
Chain | Residue |
D | CYS339 |
D | CYS342 |
D | CYS358 |
D | CYS370 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE AQH D 502 |
Chain | Residue |
D | THR107 |
D | LEU108 |
D | GLY109 |
D | PHE187 |
D | GLN224 |
D | SER225 |
D | THR226 |
D | LYS230 |
D | ILE255 |
D | ASP256 |
D | ARG257 |
D | LEU281 |
D | LEU283 |
D | ARG286 |
D | PRO300 |
D | SER301 |
D | GLY302 |
D | LEU303 |
D | TRP305 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE E 501 |
Chain | Residue |
E | CYS339 |
E | CYS342 |
E | CYS358 |
E | CYS370 |
site_id | BC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AQH E 502 |
Chain | Residue |
E | PHE187 |
E | GLN224 |
E | THR226 |
E | LYS230 |
E | ILE255 |
E | ARG257 |
E | LEU281 |
E | LEU283 |
E | ARG286 |
E | PRO300 |
E | SER301 |
E | GLY302 |
E | GLU326 |
E | THR107 |
E | LEU108 |
E | GLY109 |
E | ALA110 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE H 501 |
Chain | Residue |
H | CYS339 |
H | CYS342 |
H | CYS358 |
H | CYS370 |
site_id | BC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE AQH H 502 |
Chain | Residue |
H | LEU108 |
H | GLY109 |
H | ALA110 |
H | PHE187 |
H | GLN224 |
H | SER225 |
H | THR226 |
H | LYS230 |
H | ARG257 |
H | LEU281 |
H | LEU283 |
H | ARG286 |
H | PRO300 |
H | SER301 |
H | GLY302 |
H | LEU303 |
H | PHE320 |
H | TRP343 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE B 501 |
Chain | Residue |
B | CYS339 |
B | CYS342 |
B | CYS358 |
B | CYS370 |
site_id | BC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE AQH B 502 |
Chain | Residue |
B | THR107 |
B | GLY109 |
B | ALA110 |
B | PHE187 |
B | GLN224 |
B | THR226 |
B | LYS230 |
B | ILE255 |
B | ASP256 |
B | ARG257 |
B | LEU281 |
B | LEU283 |
B | ARG286 |
B | PRO300 |
B | SER301 |
B | GLY302 |
B | TRP305 |
B | PHE320 |
B | SER321 |
B | GLU326 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE F 501 |
Chain | Residue |
F | CYS339 |
F | CYS342 |
F | CYS358 |
F | CYS370 |
site_id | BC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE AQH F 502 |
Chain | Residue |
F | THR107 |
F | LEU108 |
F | GLY109 |
F | ALA110 |
F | PHE187 |
F | GLN224 |
F | SER225 |
F | THR226 |
F | LYS230 |
F | ASP256 |
F | ARG257 |
F | LEU281 |
F | LEU283 |
F | ARG286 |
F | PRO300 |
F | SER301 |
F | GLY302 |
F | TRP305 |
F | GLU326 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE G 501 |
Chain | Residue |
G | CYS339 |
G | CYS342 |
G | CYS358 |
G | CYS370 |
site_id | CC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE AQH G 502 |
Chain | Residue |
G | THR107 |
G | LEU108 |
G | ALA110 |
G | PHE187 |
G | THR226 |
G | LYS230 |
G | ASP256 |
G | ARG257 |
G | LEU281 |
G | ARG286 |
G | PRO300 |
G | SER301 |
G | GLY302 |
G | GLU326 |
G | TRP343 |
site_id | CC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE I 501 |
Chain | Residue |
I | CYS339 |
I | CYS342 |
I | CYS358 |
I | CYS370 |
site_id | CC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO I 502 |
Chain | Residue |
I | ARG189 |
I | GLU201 |
site_id | CC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AQH I 503 |
Chain | Residue |
I | THR107 |
I | LEU108 |
I | GLY109 |
I | ALA110 |
I | PHE187 |
I | GLN224 |
I | SER225 |
I | THR226 |
I | LYS230 |
I | ASP256 |
I | ARG257 |
I | ARG286 |
I | PRO300 |
I | SER301 |
I | GLY302 |
I | PHE320 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE J 501 |
Chain | Residue |
J | CYS339 |
J | CYS342 |
J | CYS358 |
J | CYS370 |
site_id | CC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO J 502 |
Chain | Residue |
J | ARG189 |
J | ARG200 |
J | GLU201 |
site_id | CC7 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AQH J 503 |
Chain | Residue |
J | THR107 |
J | LEU108 |
J | GLY109 |
J | ALA110 |
J | PHE187 |
J | THR226 |
J | LYS230 |
J | ARG257 |
J | LEU281 |
J | ARG286 |
J | PRO300 |
J | SER301 |
J | GLY302 |
J | LEU303 |
J | TRP305 |
J | GLU326 |
J | TRP343 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE A 501 |
Chain | Residue |
A | CYS339 |
A | CYS342 |
A | CYS358 |
A | CYS370 |
site_id | CC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE AQH A 502 |
Chain | Residue |
A | THR107 |
A | GLY109 |
A | ALA110 |
A | PHE187 |
A | SER225 |
A | THR226 |
A | LYS230 |
A | ARG257 |
A | LEU281 |
A | ARG286 |
A | PRO300 |
A | SER301 |
A | GLY302 |
A | GLU326 |