6S4G
Crystal structure of the omega transaminase from Chromobacterium violaceum in complex with PMP
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 PMP A 501 |
| Chain | Residue |
| A | SER119 |
| A | ILE262 |
| A | LYS288 |
| A | EDO502 |
| A | HOH610 |
| A | HOH613 |
| A | HOH636 |
| A | HOH639 |
| B | PHE320 |
| B | THR321 |
| A | GLY120 |
| A | SER121 |
| A | TYR153 |
| A | HIS154 |
| A | GLY155 |
| A | GLU226 |
| A | ASP259 |
| A | VAL261 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | TYR153 |
| A | ARG416 |
| A | PMP501 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue PMP B 501 |
| Chain | Residue |
| A | PHE320 |
| A | THR321 |
| B | SER119 |
| B | GLY120 |
| B | SER121 |
| B | TYR153 |
| B | HIS154 |
| B | GLY155 |
| B | GLU226 |
| B | ASP259 |
| B | VAL261 |
| B | ILE262 |
| B | LYS288 |
| B | HOH606 |
| B | HOH664 |
| B | HOH681 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | PHE22 |
| B | TYR168 |
| B | ARG416 |
| B | HOH603 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PEG B 503 |
| Chain | Residue |
| B | ASN151 |
| B | MET166 |
| B | TYR168 |
| B | ALA231 |
| B | GLY232 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | binding site for residue PMP C 501 |
| Chain | Residue |
| C | SER119 |
| C | GLY120 |
| C | SER121 |
| C | TYR153 |
| C | HIS154 |
| C | GLY155 |
| C | GLU226 |
| C | ASP259 |
| C | VAL261 |
| C | ILE262 |
| C | LYS288 |
| C | PEG502 |
| C | HOH621 |
| C | HOH640 |
| C | HOH666 |
| C | HOH693 |
| D | PHE320 |
| D | THR321 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue PEG C 502 |
| Chain | Residue |
| C | TRP60 |
| C | TYR168 |
| C | ALA231 |
| C | ARG416 |
| C | PMP501 |
| D | PHE88 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | binding site for residue PMP D 501 |
| Chain | Residue |
| C | PHE320 |
| C | THR321 |
| D | SER119 |
| D | GLY120 |
| D | SER121 |
| D | TYR153 |
| D | HIS154 |
| D | GLY155 |
| D | GLU226 |
| D | ASP259 |
| D | VAL261 |
| D | ILE262 |
| D | LYS288 |
| D | HOH618 |
| D | HOH623 |
| D | HOH631 |
| D | HOH675 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| D | TYR168 |
| D | ARG416 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 503 |
| Chain | Residue |
| D | ASN151 |
| D | GLY165 |
| D | MET166 |
| D | LYS167 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 504 |
| Chain | Residue |
| D | ASN151 |
| D | TYR168 |
| D | ALA231 |
| D | GLY232 |
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 |
