5U23
X-ray structure of the WlaRG aminotransferase from Campylobacter jejuni 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 | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0000271 | biological_process | polysaccharide biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0000271 | biological_process | polysaccharide biosynthetic process |
| D | 0008483 | molecular_function | transaminase 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 C 401 |
| Chain | Residue |
| C | HOH526 |
| C | HOH642 |
| C | HOH738 |
| D | HOH531 |
| D | HOH645 |
| D | HOH690 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | binding site for residue TQP C 402 |
| Chain | Residue |
| C | GLY58 |
| C | LEU59 |
| C | TYR84 |
| C | ALA86 |
| C | ASP155 |
| C | ALA157 |
| C | GLN158 |
| C | SER179 |
| C | TYR181 |
| C | LYS184 |
| C | ILE303 |
| C | HIS305 |
| C | TYR306 |
| C | HOH508 |
| C | HOH559 |
| C | HOH572 |
| C | HOH598 |
| C | HOH618 |
| C | HOH620 |
| C | HOH656 |
| C | HOH739 |
| C | HOH784 |
| D | GLY28 |
| D | TRP29 |
| D | TYR30 |
| D | TYR212 |
| D | LYS217 |
| D | ASN226 |
| C | LEU4 |
| C | LEU6 |
| C | ASN57 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 403 |
| Chain | Residue |
| C | LYS45 |
| C | TYR46 |
| C | ARG168 |
| C | HOH592 |
| C | HOH813 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue EDO C 404 |
| Chain | Residue |
| B | GLN260 |
| C | ILE105 |
| C | ASN106 |
| C | THR107 |
| C | TYR108 |
| C | PRO270 |
| C | SER271 |
| C | HOH541 |
| C | HOH655 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 405 |
| Chain | Residue |
| C | THR120 |
| C | LYS121 |
| C | LYS344 |
| C | GLU345 |
| C | HOH502 |
| C | HOH564 |
| C | HOH672 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CL C 406 |
| Chain | Residue |
| C | TYR294 |
| C | HIS298 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue MPO C 407 |
| Chain | Residue |
| C | ILE119 |
| C | THR120 |
| C | LYS121 |
| C | THR123 |
| C | LYS124 |
| C | TYR148 |
| C | ASN149 |
| C | HOH616 |
| C | HOH754 |
| site_id | AC8 |
| Number of Residues | 29 |
| Details | binding site for residue TQP D 401 |
| Chain | Residue |
| C | GLY28 |
| C | TRP29 |
| C | TYR30 |
| C | TYR212 |
| C | LYS217 |
| C | ASN226 |
| D | PHE3 |
| 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 | LYS184 |
| D | HIS305 |
| D | TYR306 |
| D | HOH502 |
| D | HOH554 |
| D | HOH557 |
| D | HOH635 |
| D | HOH720 |
| D | HOH737 |
| D | HOH761 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 402 |
| Chain | Residue |
| D | LEU4 |
| D | ASN5 |
| D | SER340 |
| D | PHE2 |
| site_id | AD1 |
| Number of Residues | 34 |
| Details | binding site for residue TQP A 401 |
| Chain | Residue |
| A | PHE3 |
| A | LEU4 |
| A | LEU6 |
| A | ASN57 |
| A | GLY58 |
| A | LEU59 |
| A | TYR84 |
| A | ALA86 |
| A | ASP155 |
| A | ALA157 |
| A | GLN158 |
| A | SER179 |
| A | TYR181 |
| A | LYS184 |
| A | ILE303 |
| A | HIS305 |
| A | TYR306 |
| A | HOH507 |
| A | HOH541 |
| A | HOH554 |
| A | HOH621 |
| A | HOH671 |
| A | HOH702 |
| A | HOH717 |
| A | HOH739 |
| A | HOH741 |
| A | HOH778 |
| B | GLY28 |
| B | TRP29 |
| B | TYR30 |
| B | ILE31 |
| B | TYR212 |
| B | LYS217 |
| B | ASN226 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | LYS45 |
| A | TYR46 |
| A | ARG168 |
| A | HOH750 |
| A | HOH756 |
| D | ASP166 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 401 |
| Chain | Residue |
| A | HOH535 |
| A | HOH647 |
| A | HOH706 |
| B | HOH534 |
| B | HOH558 |
| B | HOH742 |
| site_id | AD4 |
| Number of Residues | 29 |
| Details | binding site for residue TQP B 402 |
| Chain | Residue |
| A | GLY28 |
| A | TRP29 |
| A | TYR30 |
| A | TYR212 |
| A | LYS217 |
| A | ASN226 |
| B | PHE3 |
| B | LEU6 |
| B | ASN57 |
| B | GLY58 |
| B | LEU59 |
| B | TYR84 |
| B | ALA86 |
| B | ASP155 |
| B | ALA157 |
| B | GLN158 |
| B | SER179 |
| B | TYR181 |
| B | LYS184 |
| B | ILE303 |
| B | HIS305 |
| B | TYR306 |
| B | HOH512 |
| B | HOH553 |
| B | HOH640 |
| B | HOH645 |
| B | HOH662 |
| B | HOH765 |
| B | HOH772 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | LYS45 |
| B | TYR46 |
| B | ARG168 |
| B | HOH683 |
| B | HOH760 |
| site_id | AD6 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | ILE105 |
| B | ASN106 |
| B | THR107 |
| B | TYR108 |
| B | PRO270 |
| B | SER271 |
| B | HOH615 |
| B | HOH669 |
| C | GLN260 |
