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 |
