5U24
X-ray structure of the WlaRG aminotransferase from campylobacter jejuni, K184A mutant in complex with TDP-Fuc3N
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 | HOH535 |
| A | HOH547 |
| A | HOH619 |
| A | HOH760 |
| B | HOH605 |
| B | HOH635 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | binding site for residue 7SG 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 | HOH542 |
| A | HOH551 |
| A | HOH565 |
| A | HOH597 |
| A | HOH603 |
| A | HOH663 |
| A | HOH687 |
| A | HOH704 |
| A | HOH770 |
| A | HOH788 |
| 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 | HOH554 |
| 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 | HOH541 |
| A | HOH577 |
| D | GLN260 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | THR120 |
| A | LYS121 |
| A | LYS344 |
| A | GLU345 |
| A | HOH501 |
| A | HOH717 |
| A | HOH754 |
| 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 | 28 |
| Details | binding site for residue 7SG B 401 |
| Chain | Residue |
| A | GLY28 |
| A | TRP29 |
| A | TYR30 |
| A | TYR212 |
| A | LYS217 |
| A | ASN226 |
| B | LEU4 |
| B | LEU6 |
| B | ASN57 |
| B | GLY58 |
| B | LEU59 |
| B | TYR84 |
| B | ALA86 |
| B | ASP155 |
| B | ALA157 |
| B | GLN158 |
| B | SER179 |
| B | TYR181 |
| B | ILE303 |
| B | HIS305 |
| B | TYR306 |
| B | HOH558 |
| B | HOH571 |
| B | HOH645 |
| B | HOH657 |
| B | HOH701 |
| B | HOH758 |
| B | HOH762 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | PHE2 |
| B | PHE3 |
| B | LEU4 |
| B | ASN5 |
| B | SER340 |
| B | HOH679 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | LYS45 |
| B | TYR46 |
| B | ARG168 |
| B | HOH781 |
| C | ASP166 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 401 |
| Chain | Residue |
| D | HOH565 |
| D | HOH621 |
| D | HOH669 |
| C | HOH516 |
| C | HOH655 |
| C | HOH684 |
| site_id | AD2 |
| Number of Residues | 30 |
| Details | binding site for residue 7SG C 402 |
| Chain | Residue |
| C | LEU4 |
| C | LEU6 |
| C | ASN57 |
| C | GLY58 |
| C | LEU59 |
| C | TYR84 |
| C | ASP155 |
| C | ALA157 |
| C | GLN158 |
| C | SER179 |
| C | TYR181 |
| C | ILE303 |
| C | HIS305 |
| C | TYR306 |
| C | HOH523 |
| C | HOH529 |
| C | HOH532 |
| C | HOH640 |
| C | HOH647 |
| C | HOH664 |
| C | HOH689 |
| C | HOH712 |
| C | HOH758 |
| D | GLY28 |
| D | TRP29 |
| D | TYR30 |
| D | TYR212 |
| D | LYS217 |
| D | ASN226 |
| D | HOH622 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 403 |
| Chain | Residue |
| B | ASP166 |
| C | LYS45 |
| C | TYR46 |
| C | ARG168 |
| C | HOH790 |
| site_id | AD4 |
| Number of Residues | 27 |
| Details | binding site for residue 7SG D 401 |
| Chain | Residue |
| C | GLY28 |
| C | TRP29 |
| C | TYR30 |
| C | TYR212 |
| C | LYS217 |
| C | ASN226 |
| D | LEU6 |
| D | ASN57 |
| D | GLY58 |
| D | LEU59 |
| D | TYR84 |
| D | ASP155 |
| D | ALA157 |
| D | GLN158 |
| D | SER179 |
| D | TYR181 |
| D | ILE303 |
| D | HIS305 |
| D | TYR306 |
| D | HOH519 |
| D | HOH554 |
| D | HOH611 |
| D | HOH673 |
| D | HOH696 |
| D | HOH705 |
| D | HOH706 |
| D | HOH728 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 402 |
| Chain | Residue |
| D | LYS45 |
| D | TYR46 |
| D | ARG168 |
| D | HOH720 |
| D | HOH729 |
| site_id | AD6 |
| 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 | HOH580 |
| D | HOH589 |
