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 | 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 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 |