Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1475 |
| Chain | Residue |
| A | PHE56 |
| B | TYR89 |
| A | LEU59 |
| A | TYR148 |
| A | TYR164 |
| A | LYS298 |
| A | VAL436 |
| A | PLP1298 |
| A | HOH2063 |
| B | THR88 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1476 |
| Chain | Residue |
| A | GLU428 |
| A | LYS429 |
| A | ASP459 |
| A | TYR463 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG A 1477 |
| Chain | Residue |
| A | ARG256 |
| A | LYS260 |
| A | GLN290 |
| A | PRO291 |
| A | ASP292 |
| A | HOH2268 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1478 |
| Chain | Residue |
| A | PHE176 |
| A | SER177 |
| A | HOH2194 |
| B | ASN137 |
| C | ALA178 |
| D | ASN137 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE A 1479 |
| Chain | Residue |
| A | TYR135 |
| A | GLY263 |
| A | GLU315 |
| A | HOH2146 |
| A | HOH2252 |
| A | HOH2371 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PEG B 1475 |
| Chain | Residue |
| A | PHE25 |
| A | SER26 |
| A | HOH2026 |
| A | HOH2335 |
| B | ARG324 |
| B | HOH2231 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGE B 1476 |
| Chain | Residue |
| B | TYR135 |
| B | ARG138 |
| B | GLY263 |
| B | LEU265 |
| B | GLU315 |
| B | HOH2106 |
| B | HOH2234 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B 1477 |
| Chain | Residue |
| B | ARG256 |
| B | LYS260 |
| B | GLN290 |
| B | PRO291 |
| B | ASP292 |
| B | GLU315 |
| B | HOH2235 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 B 1478 |
| Chain | Residue |
| A | THR88 |
| A | TYR89 |
| A | HOH2093 |
| B | VAL34 |
| B | PHE56 |
| B | LEU59 |
| B | VAL436 |
| B | HOH2020 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PEG C 1475 |
| Chain | Residue |
| C | ARG256 |
| C | LYS260 |
| C | GLN290 |
| C | PRO291 |
| C | ASP292 |
| C | GLU315 |
| C | PG41478 |
| C | HOH2039 |
| C | HOH2209 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 C 1476 |
| Chain | Residue |
| A | ASN137 |
| B | SER177 |
| C | ASN137 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 C 1477 |
| Chain | Residue |
| C | PHE56 |
| C | LEU59 |
| C | VAL436 |
| C | HOH2057 |
| D | THR88 |
| D | TYR89 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 C 1478 |
| Chain | Residue |
| C | TYR135 |
| C | ARG138 |
| C | GLY263 |
| C | GLU315 |
| C | PEG1475 |
| C | HOH2133 |
| C | HOH2208 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PG4 C 1479 |
| Chain | Residue |
| C | LYS429 |
| C | ASP459 |
| C | TYR463 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 1PE D 1475 |
| Chain | Residue |
| C | THR88 |
| C | TYR89 |
| C | HOH2085 |
| D | PHE56 |
| D | LEU59 |
| D | TYR164 |
| D | LEU272 |
| D | VAL436 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PGE D 1476 |
| Chain | Residue |
| D | GLU315 |
| D | HOH2081 |
| D | HOH2138 |
| D | HOH2204 |
| D | TYR135 |
| D | GLY263 |
| D | LEU265 |
| site_id | BC8 |
| Number of Residues | 24 |
| Details | Binding site for Di-peptide LYS A 298 and PLP A1298 |
| Chain | Residue |
| A | LEU59 |
| A | CYS61 |
| A | GLY121 |
| A | SER122 |
| A | TYR148 |
| A | HIS149 |
| A | GLU237 |
| A | ASP269 |
| A | VAL271 |
| A | LEU272 |
| A | GLY297 |
| A | GLY299 |
| A | LEU300 |
| A | SER301 |
| A | SER302 |
| A | SER303 |
| A | 1PE1475 |
| A | HOH2136 |
| A | HOH2160 |
| A | HOH2240 |
| A | HOH2272 |
| A | HOH2369 |
| B | THR330 |
| B | TYR331 |
| site_id | BC9 |
| Number of Residues | 23 |
| Details | Binding site for Di-peptide LYS B 298 and PLP B1298 |
| Chain | Residue |
| A | THR330 |
| A | TYR331 |
| A | HOH2137 |
| A | HOH2290 |
| A | HOH2291 |
| B | LEU59 |
| B | CYS61 |
| B | GLY121 |
| B | SER122 |
| B | TYR148 |
| B | HIS149 |
| B | GLU237 |
| B | ASP269 |
| B | VAL271 |
| B | LEU272 |
| B | GLY297 |
| B | GLY299 |
| B | LEU300 |
| B | SER301 |
| B | SER302 |
| B | SER303 |
| B | HOH2160 |
| B | HOH2188 |
| site_id | CC1 |
| Number of Residues | 25 |
| Details | Binding site for Di-peptide LYS C 298 and PLP C1298 |
| Chain | Residue |
| C | LEU59 |
| C | CYS61 |
| C | GLY121 |
| C | SER122 |
| C | TYR148 |
| C | HIS149 |
| C | GLY150 |
| C | GLU237 |
| C | ASP269 |
| C | VAL271 |
| C | LEU272 |
| C | GLY297 |
| C | GLY299 |
| C | LEU300 |
| C | SER301 |
| C | SER302 |
| C | SER303 |
| C | HOH2123 |
| C | HOH2149 |
| C | HOH2197 |
| C | HOH2226 |
| C | HOH2228 |
| C | HOH2285 |
| D | THR330 |
| D | TYR331 |
| site_id | CC2 |
| Number of Residues | 24 |
| Details | Binding site for Di-peptide LYS D 298 and PLP D1298 |
| Chain | Residue |
| C | THR330 |
| C | TYR331 |
| C | HOH2124 |
| C | HOH2247 |
| C | HOH2248 |
| C | HOH2250 |
| D | LEU59 |
| D | CYS61 |
| D | GLY121 |
| D | SER122 |
| D | TYR148 |
| D | HIS149 |
| D | GLU237 |
| D | ASP269 |
| D | VAL271 |
| D | LEU272 |
| D | GLY297 |
| D | GLY299 |
| D | LEU300 |
| D | SER301 |
| D | SER302 |
| D | SER303 |
| D | HOH2128 |
| D | HOH2153 |
Functional Information from PROSITE/UniProt
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TMGKGLSSSS |
| Chain | Residue | Details |
| A | THR295-SER304 | |
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. WInDEVlt.GFgRtGkwfgyqhygvqp....DIItmGKglsSS |
| Chain | Residue | Details |
| A | TRP266-SER303 | |
