5U21
X-ray structure of the WlaRF aminotransferase from Campylobacter jejuni, K184A mutant in complex with TDP-Qui3N
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0000271 | biological_process | polysaccharide biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0000271 | biological_process | polysaccharide biosynthetic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 401 |
| Chain | Residue |
| A | HOH523 |
| A | HOH695 |
| A | HOH733 |
| B | HOH539 |
| B | HOH607 |
| B | HOH723 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | binding site for residue TQP A 402 |
| Chain | Residue |
| A | LEU59 |
| A | TYR84 |
| A | ASP155 |
| A | ALA157 |
| A | GLN158 |
| A | SER179 |
| A | TYR181 |
| A | ILE303 |
| A | HIS305 |
| A | TYR306 |
| A | HOH519 |
| A | HOH571 |
| A | HOH643 |
| A | HOH644 |
| A | HOH660 |
| A | HOH666 |
| A | HOH698 |
| A | HOH704 |
| A | HOH715 |
| B | GLY28 |
| B | TRP29 |
| B | TYR30 |
| B | TYR212 |
| B | LYS217 |
| B | ASN226 |
| A | LEU6 |
| A | ASN57 |
| A | GLY58 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | LYS45 |
| A | TYR46 |
| A | ARG168 |
| A | HOH697 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | ILE105 |
| A | ASN106 |
| A | THR107 |
| A | TYR108 |
| A | PRO270 |
| A | SER271 |
| A | HOH551 |
| A | HOH576 |
| D | GLN260 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | THR120 |
| A | LYS121 |
| A | GLU345 |
| A | HOH506 |
| A | HOH761 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 406 |
| Chain | Residue |
| A | TYR294 |
| A | HIS298 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | binding site for residue TQP B 401 |
| Chain | Residue |
| A | GLY28 |
| A | TRP29 |
| A | TYR30 |
| A | TYR212 |
| A | LYS217 |
| A | ASN226 |
| B | PHE3 |
| B | LEU4 |
| B | LEU6 |
| B | ASN57 |
| B | GLY58 |
| B | LEU59 |
| B | TYR84 |
| B | ASP155 |
| B | ALA157 |
| B | GLN158 |
| B | SER179 |
| B | TYR181 |
| B | ILE303 |
| B | HIS305 |
| B | TYR306 |
| B | HOH520 |
| B | HOH558 |
| B | HOH575 |
| B | HOH584 |
| B | HOH655 |
| B | HOH679 |
| B | HOH741 |
| B | HOH747 |
| B | HOH748 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | PHE2 |
| B | PHE3 |
| B | ASN5 |
| B | SER340 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 401 |
| Chain | Residue |
| C | HOH576 |
| C | HOH643 |
| C | HOH706 |
| D | HOH584 |
| D | HOH633 |
| D | HOH745 |
| site_id | AD1 |
| Number of Residues | 33 |
| Details | binding site for residue TQP C 402 |
| Chain | Residue |
| C | LEU59 |
| C | TYR84 |
| C | ALA86 |
| C | ASP155 |
| C | ALA157 |
| C | GLN158 |
| C | SER179 |
| C | TYR181 |
| C | ILE303 |
| C | HIS305 |
| C | TYR306 |
| C | HOH512 |
| C | HOH514 |
| C | HOH551 |
| C | HOH627 |
| C | HOH673 |
| C | HOH684 |
| C | HOH688 |
| C | HOH690 |
| C | HOH724 |
| C | HOH734 |
| C | HOH765 |
| D | GLY28 |
| D | TRP29 |
| D | TYR30 |
| D | TYR212 |
| D | LYS217 |
| D | ASN226 |
| C | PHE3 |
| C | LEU4 |
| C | LEU6 |
| C | ASN57 |
| C | GLY58 |
| site_id | AD2 |
| Number of Residues | 32 |
| Details | binding site for residue TQP D 401 |
| Chain | Residue |
| C | GLY28 |
| C | TRP29 |
| C | TYR30 |
| C | TYR212 |
| C | LYS217 |
| C | ASN226 |
| D | LEU4 |
| D | LEU6 |
| D | ASN57 |
| D | GLY58 |
| D | LEU59 |
| D | TYR84 |
| D | ALA86 |
| D | ASP155 |
| D | ALA157 |
| D | GLN158 |
| D | SER179 |
| D | TYR181 |
| D | ILE303 |
| D | HIS305 |
| D | TYR306 |
| D | HOH517 |
| D | HOH555 |
| D | HOH572 |
| D | HOH634 |
| D | HOH640 |
| D | HOH646 |
| D | HOH697 |
| D | HOH704 |
| D | HOH732 |
| D | HOH744 |
| D | HOH764 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 402 |
| Chain | Residue |
| D | LYS45 |
| D | TYR46 |
| D | ARG168 |
| D | HOH600 |
| D | HOH769 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 403 |
| Chain | Residue |
| D | ILE105 |
| D | ASN106 |
| D | THR107 |
| D | TYR108 |
| D | PRO270 |
| D | SER271 |
| D | HOH585 |
| D | HOH658 |
