4UOY
Crystal structure of YgjG in complex with Pyridoxal-5'-phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009447 | biological_process | putrescine catabolic process |
| A | 0019161 | molecular_function | diamine transaminase activity |
| A | 0019477 | biological_process | L-lysine catabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033094 | molecular_function | putrescine--2-oxoglutarate transaminase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009447 | biological_process | putrescine catabolic process |
| B | 0019161 | molecular_function | diamine transaminase activity |
| B | 0019477 | biological_process | L-lysine catabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033094 | molecular_function | putrescine--2-oxoglutarate transaminase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009447 | biological_process | putrescine catabolic process |
| C | 0019161 | molecular_function | diamine transaminase activity |
| C | 0019477 | biological_process | L-lysine catabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0033094 | molecular_function | putrescine--2-oxoglutarate transaminase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009447 | biological_process | putrescine catabolic process |
| D | 0019161 | molecular_function | diamine transaminase activity |
| D | 0019477 | biological_process | L-lysine catabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0033094 | molecular_function | putrescine--2-oxoglutarate transaminase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 800 |
| Chain | Residue |
| A | SER149 |
| A | GLN274 |
| A | LYS300 |
| A | HOH2046 |
| A | HOH2084 |
| A | HOH2096 |
| A | HOH2097 |
| B | THR332 |
| A | GLY150 |
| A | THR151 |
| A | PHE180 |
| A | HIS181 |
| A | GLY182 |
| A | GLU238 |
| A | ASP271 |
| A | VAL273 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 800 |
| Chain | Residue |
| A | THR332 |
| A | HOH2028 |
| A | HOH2030 |
| B | SER149 |
| B | GLY150 |
| B | THR151 |
| B | PHE180 |
| B | HIS181 |
| B | GLU238 |
| B | ASP271 |
| B | VAL273 |
| B | GLN274 |
| B | LYS300 |
| B | HOH2057 |
| B | HOH2065 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP C 800 |
| Chain | Residue |
| C | SER149 |
| C | GLY150 |
| C | THR151 |
| C | PHE180 |
| C | HIS181 |
| C | GLY182 |
| C | GLU238 |
| C | GLU243 |
| C | ASP271 |
| C | VAL273 |
| C | GLN274 |
| C | LYS300 |
| C | HOH2042 |
| C | HOH2058 |
| C | HOH2077 |
| C | HOH2106 |
| D | THR331 |
| D | THR332 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP D 800 |
| Chain | Residue |
| C | THR332 |
| C | HOH2041 |
| C | HOH2044 |
| D | SER149 |
| D | GLY150 |
| D | THR151 |
| D | PHE180 |
| D | HIS181 |
| D | GLY182 |
| D | GLU238 |
| D | ASP271 |
| D | VAL273 |
| D | GLN274 |
| D | LYS300 |
| D | HOH2022 |
| D | HOH2034 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 1461 |
| Chain | Residue |
| A | GLN119 |
| A | LEU121 |
| A | ASP123 |
| A | HOH2098 |
| B | PHE50 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1460 |
| Chain | Residue |
| A | PHE50 |
| B | HIS117 |
| B | GLN119 |
| B | LEU121 |
| B | ASP123 |
| B | ARG126 |
| B | HOH2075 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. MIlDEVqt.GMgRtGkmfacehenvqp....DILclAKalgGG |
| Chain | Residue | Details |
| A | MET268-GLY305 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: in other chain => ECO:0000269|PubMed:25423189 |
| Chain | Residue | Details |
| C | GLY150 | |
| C | GLN274 | |
| D | GLY150 | |
| D | GLN274 | |
| A | GLY150 | |
| A | GLN274 | |
| B | GLY150 | |
| B | GLN274 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:25423189 |
| Chain | Residue | Details |
| A | THR332 | |
| B | THR332 | |
| C | THR332 | |
| D | THR332 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:25423189, ECO:0007744|PDB:4UOY |
| Chain | Residue | Details |
| A | LYS300 | |
| B | LYS300 | |
| C | LYS300 | |
| D | LYS300 |
