2COI
Crystal structure of oxidized 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 | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1430 |
Chain | Residue |
B | ASP133 |
B | HOH1477 |
B | HOH1745 |
B | HOH1746 |
B | HOH1747 |
B | HOH1748 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP A 410 |
Chain | Residue |
A | TYR227 |
A | GLU257 |
A | THR260 |
A | LEU286 |
A | GLY288 |
A | VAL289 |
A | THR290 |
A | THR333 |
A | HOH430 |
A | HOH461 |
A | HOH575 |
A | ARG119 |
A | ARG212 |
A | LYS222 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PLP B 410 |
Chain | Residue |
B | ARG119 |
B | ARG212 |
B | LYS222 |
B | TYR227 |
B | GLU257 |
B | THR260 |
B | ASN262 |
B | LEU286 |
B | GLY288 |
B | VAL289 |
B | THR290 |
B | GLY332 |
B | THR333 |
B | HOH1442 |
B | HOH1445 |
B | HOH1449 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GBN A 420 |
Chain | Residue |
A | TYR161 |
A | ARG163 |
A | TYR193 |
A | THR260 |
A | GLY332 |
A | THR333 |
A | ALA334 |
A | HOH508 |
A | HOH555 |
A | HOH560 |
B | TYR90 |
B | VAL175 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GBN B 420 |
Chain | Residue |
A | TYR90 |
A | VAL175 |
B | TYR161 |
B | ARG163 |
B | TYR193 |
B | THR260 |
B | MET261 |
B | GLY332 |
B | THR333 |
B | ALA334 |
B | HOH1455 |
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 |