4AH3
Crystal structure of the holo omega-transaminase from Chromobacterium violaceum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP A 1288 |
| Chain | Residue |
| A | SER119 |
| A | LYS288 |
| A | HOH2138 |
| A | HOH2389 |
| A | HOH2475 |
| A | HOH2538 |
| A | HOH2722 |
| C | PHE320 |
| C | THR321 |
| C | HOH2297 |
| A | GLY120 |
| A | SER121 |
| A | TYR153 |
| A | GLY155 |
| A | GLU226 |
| A | ASP259 |
| A | VAL261 |
| A | ILE262 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP B 1288 |
| Chain | Residue |
| B | SER119 |
| B | GLY120 |
| B | SER121 |
| B | TYR153 |
| B | HIS154 |
| B | GLY155 |
| B | GLU226 |
| B | ASP259 |
| B | VAL261 |
| B | ILE262 |
| B | LYS288 |
| B | HOH2264 |
| B | HOH2348 |
| B | HOH2408 |
| B | HOH2410 |
| B | HOH2560 |
| D | PHE320 |
| D | THR321 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP C 1288 |
| Chain | Residue |
| A | PHE320 |
| A | THR321 |
| A | HOH2299 |
| A | HOH2555 |
| A | HOH2556 |
| C | SER119 |
| C | GLY120 |
| C | SER121 |
| C | TYR153 |
| C | GLY155 |
| C | GLU226 |
| C | ASP259 |
| C | VAL261 |
| C | ILE262 |
| C | LYS288 |
| C | HOH2250 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP D 1288 |
| Chain | Residue |
| B | PHE320 |
| B | THR321 |
| B | HOH2195 |
| B | HOH2430 |
| B | HOH2431 |
| B | HOH2432 |
| D | SER119 |
| D | GLY120 |
| D | SER121 |
| D | TYR153 |
| D | HIS154 |
| D | GLY155 |
| D | GLU226 |
| D | ASP259 |
| D | VAL261 |
| D | ILE262 |
| D | LYS288 |
| D | HOH2160 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVaDEVic.GFgRtGewfghqhfgfqp....DLFtaAKglsSG |
| Chain | Residue | Details |
| A | LEU256-GLY293 |
