Structure of PDB 2hdk Chain B Binding Site BS02

Receptor Information
>2hdk Chain B (length=363) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPR
IQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLR
SAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPS
LGVSQPRRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYK
LGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDG
VLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRALEE
GRVREVFGSGTAAQVAPVHRILYKDRNLHIPTMENGPELILRFQKELKEI
QYGIRAHEWMFPV
Ligand information
Ligand IDCOI
InChIInChI=1S/C6H10O3/c1-4(2)3-5(7)6(8)9/h4H,3H2,1-2H3,(H,8,9)
InChIKeyBKAJNAXTPSGJCU-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01O=C(C(=O)O)CC(C)C
OpenEye OEToolkits 1.7.6CC(C)CC(=O)C(=O)O
CACTVS 3.370CC(C)CC(=O)C(O)=O
FormulaC6 H10 O3
Name2-OXO-4-METHYLPENTANOIC ACID;
alpha-ketoisocaproic acid
ChEMBLCHEMBL445647
DrugBankDB03229
ZINCZINC000001532578
PDB chain2hdk Chain B Residue 900 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2hdk Human Mitochondrial Branched Chain Aminotransferase Isozyme: STRUCTURAL ROLE OF THE CXXC CENTER IN CATALYSIS.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		G812 T813 A814
Binding residue
(residue number reindexed from 1)		G310 T311 A312
Annotation score5
Binding affinityMOAD: Kd=6.1mM
Enzymatic activity
Catalytic site (original residue number in PDB) K702
Catalytic site (residue number reindexed from 1) K200
Enzyme Commision number 2.6.1.42: branched-chain-amino-acid transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004084 branched-chain-amino-acid transaminase activity
GO:0005515 protein binding
GO:0008483 transaminase activity
GO:0052654 L-leucine-2-oxoglutarate transaminase activity
GO:0052655 L-valine-2-oxoglutarate transaminase activity
GO:0052656 L-isoleucine-2-oxoglutarate transaminase activity
Biological Process
GO:0006549 isoleucine metabolic process
GO:0006550 isoleucine catabolic process
GO:0006551 L-leucine metabolic process
GO:0006573 valine metabolic process
GO:0006629 lipid metabolic process
GO:0008652 amino acid biosynthetic process
GO:0009081 branched-chain amino acid metabolic process
GO:0009082 branched-chain amino acid biosynthetic process
GO:0009083 branched-chain amino acid catabolic process
GO:0009098 L-leucine biosynthetic process
GO:0009099 L-valine biosynthetic process
GO:0010817 regulation of hormone levels
GO:1990830 cellular response to leukemia inhibitory factor
Cellular Component
GO:0005654 nucleoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2hdk, PDBe:2hdk, PDBj:2hdk
PDBsum2hdk
PubMed17050531
UniProtO15382|BCAT2_HUMAN Branched-chain-amino-acid aminotransferase, mitochondrial (Gene Name=BCAT2)

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