2ABJ
Crystal structure of human branched chain amino acid transaminase in a complex with an inhibitor, C16H10N2O4F3SCl, and pyridoxal 5' phosphate.
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:2-oxoglutarate transaminase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0006550 | biological_process | L-isoleucine catabolic process |
| A | 0006552 | biological_process | L-leucine catabolic process |
| A | 0006574 | biological_process | L-valine catabolic process |
| A | 0009081 | biological_process | branched-chain amino acid metabolic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0052654 | molecular_function | L-leucine:2-oxoglutarate transaminase activity |
| A | 0052655 | molecular_function | L-valine:2-oxoglutarate transaminase activity |
| A | 0052656 | molecular_function | L-isoleucine:2-oxoglutarate transaminase activity |
| D | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004084 | molecular_function | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005829 | cellular_component | cytosol |
| D | 0006550 | biological_process | L-isoleucine catabolic process |
| D | 0006552 | biological_process | L-leucine catabolic process |
| D | 0006574 | biological_process | L-valine catabolic process |
| D | 0009081 | biological_process | branched-chain amino acid metabolic process |
| D | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| D | 0052654 | molecular_function | L-leucine:2-oxoglutarate transaminase activity |
| D | 0052655 | molecular_function | L-valine:2-oxoglutarate transaminase activity |
| D | 0052656 | molecular_function | L-isoleucine:2-oxoglutarate transaminase activity |
| G | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004084 | molecular_function | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005739 | cellular_component | mitochondrion |
| G | 0005829 | cellular_component | cytosol |
| G | 0006550 | biological_process | L-isoleucine catabolic process |
| G | 0006552 | biological_process | L-leucine catabolic process |
| G | 0006574 | biological_process | L-valine catabolic process |
| G | 0009081 | biological_process | branched-chain amino acid metabolic process |
| G | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| G | 0052654 | molecular_function | L-leucine:2-oxoglutarate transaminase activity |
| G | 0052655 | molecular_function | L-valine:2-oxoglutarate transaminase activity |
| G | 0052656 | molecular_function | L-isoleucine:2-oxoglutarate transaminase activity |
| J | 0000082 | biological_process | G1/S transition of mitotic cell cycle |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0004084 | molecular_function | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0005739 | cellular_component | mitochondrion |
| J | 0005829 | cellular_component | cytosol |
| J | 0006550 | biological_process | L-isoleucine catabolic process |
| J | 0006552 | biological_process | L-leucine catabolic process |
| J | 0006574 | biological_process | L-valine catabolic process |
| J | 0009081 | biological_process | branched-chain amino acid metabolic process |
| J | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| J | 0052654 | molecular_function | L-leucine:2-oxoglutarate transaminase activity |
| J | 0052655 | molecular_function | L-valine:2-oxoglutarate transaminase activity |
| J | 0052656 | molecular_function | L-isoleucine:2-oxoglutarate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CBC A 1401 |
| Chain | Residue |
| A | PHE47 |
| A | THR331 |
| A | ALA332 |
| A | CYS333 |
| A | PLP420 |
| A | HOH1746 |
| A | PHE93 |
| A | TYR159 |
| A | TYR191 |
| A | LYS220 |
| A | GLN242 |
| A | THR258 |
| A | MET259 |
| A | GLY330 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 420 |
| Chain | Residue |
| A | ARG117 |
| A | ARG210 |
| A | LYS220 |
| A | TYR225 |
| A | GLU255 |
| A | THR258 |
| A | ASN260 |
| A | LEU284 |
| A | GLY286 |
| A | VAL287 |
| A | THR288 |
| A | GLY330 |
| A | THR331 |
| A | CBC1401 |
| A | HOH1402 |
| A | HOH1403 |
| A | HOH1404 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE CBC D 2401 |
| Chain | Residue |
| A | VAL173 |
| D | PHE47 |
| D | PHE93 |
| D | TYR159 |
| D | LYS220 |
| D | GLN242 |
| D | THR258 |
| D | MET259 |
| D | GLY330 |
| D | ALA332 |
| D | CYS333 |
| D | PLP420 |
| D | HOH2454 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP D 420 |
| Chain | Residue |
| D | ARG117 |
| D | ARG210 |
| D | LYS220 |
| D | TYR225 |
| D | GLU255 |
| D | THR258 |
| D | MET259 |
| D | ASN260 |
| D | LEU284 |
| D | GLY286 |
| D | VAL287 |
| D | THR288 |
| D | THR331 |
| D | CBC2401 |
| D | HOH2405 |
| D | HOH2408 |
| D | HOH2457 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CBC G 3401 |
| Chain | Residue |
| G | PHE47 |
| G | PHE93 |
| G | TYR159 |
| G | LYS220 |
| G | GLN242 |
| G | THR258 |
| G | MET259 |
| G | GLY330 |
| G | ALA332 |
| G | CYS333 |
| G | PLP420 |
| G | HOH3444 |
| J | TYR88 |
| J | VAL173 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PLP G 420 |
| Chain | Residue |
| G | ARG117 |
| G | ARG210 |
| G | LYS220 |
| G | TYR225 |
| G | GLU255 |
| G | THR258 |
| G | MET259 |
| G | ASN260 |
| G | LEU284 |
| G | GLY286 |
| G | VAL287 |
| G | THR288 |
| G | GLY330 |
| G | THR331 |
| G | CBC3401 |
| G | HOH3406 |
| G | HOH3407 |
| G | HOH3428 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CBC J 4401 |
| Chain | Residue |
| J | GLN242 |
| J | THR258 |
| J | MET259 |
| J | GLY330 |
| J | THR331 |
| J | ALA332 |
| J | CYS333 |
| J | PLP420 |
| J | HOH4421 |
| G | VAL173 |
| J | PHE47 |
| J | PHE93 |
| J | TYR159 |
| J | TYR191 |
| J | LYS220 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP J 420 |
| Chain | Residue |
| J | ARG117 |
| J | ARG210 |
| J | LYS220 |
| J | TYR225 |
| J | GLU255 |
| J | THR258 |
| J | ASN260 |
| J | LEU284 |
| J | GLY286 |
| J | VAL287 |
| J | THR288 |
| J | THR331 |
| J | CBC4401 |
| J | HOH4402 |
| J | HOH4403 |
| J | HOH4419 |
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 | GLU255-ARG289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"16141215","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2COG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2COI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2COJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| A | LYS220 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| D | LYS220 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| G | LYS220 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| J | LYS220 |
