2COJ
Crystal structure of reduced human cytosolic branched-chain aminotransferase complexed with gabapentin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009081 | biological_process | branched-chain amino acid metabolic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0009099 | biological_process | valine biosynthetic process |
| A | 0050048 | molecular_function | L-leucine:2-oxoglutarate aminotransferase activity |
| A | 0052654 | molecular_function | L-leucine transaminase activity |
| A | 0052655 | molecular_function | L-valine transaminase activity |
| A | 0052656 | molecular_function | L-isoleucine transaminase activity |
| B | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009081 | biological_process | branched-chain amino acid metabolic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0009099 | biological_process | valine biosynthetic process |
| B | 0050048 | molecular_function | L-leucine:2-oxoglutarate aminotransferase activity |
| B | 0052654 | molecular_function | L-leucine transaminase activity |
| B | 0052655 | molecular_function | L-valine transaminase activity |
| B | 0052656 | molecular_function | L-isoleucine transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 430 |
| Chain | Residue |
| B | ASP133 |
| B | GLU274 |
| B | HOH433 |
| B | HOH442 |
| B | HOH500 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 410 |
| Chain | Residue |
| A | THR260 |
| A | LEU286 |
| A | GLY288 |
| A | VAL289 |
| A | THR290 |
| A | GLY332 |
| A | THR333 |
| A | HOH421 |
| A | HOH426 |
| A | HOH466 |
| A | ARG119 |
| A | LYS222 |
| A | TYR227 |
| A | GLU257 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 410 |
| Chain | Residue |
| B | ARG119 |
| B | ARG212 |
| B | LYS222 |
| B | TYR227 |
| B | GLU257 |
| B | THR260 |
| B | LEU286 |
| B | GLY288 |
| B | VAL289 |
| B | THR290 |
| B | THR333 |
| B | HOH432 |
| B | HOH434 |
| B | HOH477 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GBN A 420 |
| Chain | Residue |
| A | TYR161 |
| A | THR260 |
| A | MET261 |
| A | GLY332 |
| A | THR333 |
| A | ALA334 |
| A | HOH469 |
| B | TYR90 |
| B | VAL175 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GBN B 420 |
| Chain | Residue |
| A | TYR90 |
| B | TYR161 |
| B | ARG163 |
| B | THR260 |
| B | MET261 |
| B | GLY332 |
| B | THR333 |
| B | ALA334 |
| B | HOH509 |
Functional Information from PROSITE/UniProt
| site_id | PS00770 |
| Number of Residues | 35 |
| Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EvGtmNLFlywinedgeee.LaTppldgii.LpGVtR |
| Chain | Residue | Details |
| A | GLU257-ARG291 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330 |
| Chain | Residue | Details |
| A | MET1 | |
| B | MET1 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS222 | |
| B | LYS222 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| A | LYS222 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| B | LYS222 |
