3WX9
Crystal structure of Pyrococcus horikoshii kynurenine aminotransferase in complex with PMP, GLA, 4AD, 2OG, GLU and KYA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 1901605 | biological_process | alpha-amino acid metabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 1901605 | biological_process | alpha-amino acid metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PMP A 501 |
| Chain | Residue |
| A | GLY128 |
| A | SER268 |
| A | LYS269 |
| A | ARG276 |
| A | G9A503 |
| C | TYR94 |
| A | SER129 |
| A | GLN130 |
| A | TYR154 |
| A | ASN208 |
| A | ASP236 |
| A | PRO238 |
| A | TYR239 |
| A | THR266 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AKG A 502 |
| Chain | Residue |
| A | TYR115 |
| A | ASP237 |
| A | PRO238 |
| A | TYR239 |
| A | GLY240 |
| A | GLU241 |
| A | LEU242 |
| A | TYR263 |
| A | GLY265 |
| A | THR266 |
| A | ILE270 |
| A | HOH614 |
| A | HOH878 |
| A | HOH879 |
| A | HOH880 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE G9A A 503 |
| Chain | Residue |
| A | GLY64 |
| A | TYR154 |
| A | LEU155 |
| A | ALA156 |
| A | ASN208 |
| A | TYR239 |
| A | ARG400 |
| A | PMP501 |
| A | 3EE504 |
| A | HOH798 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 3EE A 504 |
| Chain | Residue |
| A | ARG47 |
| A | GLY64 |
| A | LEU65 |
| A | ARG400 |
| A | G9A503 |
| A | HOH641 |
| A | HOH881 |
| A | HOH910 |
| C | TYR94 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLU A 505 |
| Chain | Residue |
| A | SER44 |
| A | VAL46 |
| A | LEU155 |
| A | VAL384 |
| A | ALA388 |
| A | ARG393 |
| A | HOH759 |
| A | HOH822 |
| A | HOH877 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PMP C 501 |
| Chain | Residue |
| A | TYR94 |
| C | GLY128 |
| C | SER129 |
| C | GLN130 |
| C | TYR154 |
| C | VAL203 |
| C | ASN208 |
| C | ASP236 |
| C | PRO238 |
| C | TYR239 |
| C | THR266 |
| C | SER268 |
| C | LYS269 |
| C | ARG276 |
| C | G9A503 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AKG C 502 |
| Chain | Residue |
| C | TYR115 |
| C | ASP237 |
| C | GLY240 |
| C | GLU241 |
| C | LYS251 |
| C | TYR263 |
| C | GLY265 |
| C | THR266 |
| C | ILE270 |
| C | TRP279 |
| C | HOH893 |
| C | HOH894 |
| C | HOH900 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE G9A C 503 |
| Chain | Residue |
| C | ARG47 |
| C | GLY64 |
| C | TYR154 |
| C | LEU155 |
| C | ALA156 |
| C | ASN208 |
| C | TYR239 |
| C | LYS269 |
| C | ARG400 |
| C | PMP501 |
| C | 3EE504 |
| C | HOH754 |
| C | HOH755 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3EE C 504 |
| Chain | Residue |
| C | GLY63 |
| C | GLY64 |
| C | LEU65 |
| C | ARG400 |
| C | G9A503 |
| C | HOH659 |
| C | HOH896 |
| C | HOH897 |
| C | HOH1017 |
| A | TYR94 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE KYA C 505 |
| Chain | Residue |
| C | SER44 |
| C | VAL46 |
| C | ARG47 |
| C | LEU155 |
| C | GLN159 |
| C | LYS370 |
| C | ALA388 |
| C | ARG393 |
| C | HOH842 |
| C | HOH1010 |
