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 | 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 | 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 | 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 | 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 |