Structure of PDB 1olu Chain A Binding Site BS02

Receptor Information
>1olu Chain A (length=366) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PQFPGASAEFIDKLEFIQPNGIPIYRVMDRQGQIINPSEDPHLPKEKVLK
LYKSMTLLNTMDRILYESQRQGRISFYMTNYGEEGTHVGSAAALDNTDLV
FGQYREAGVLMYRDYPLELFMAQCYGNISDLGKGRQMPVHYGCKERHFVT
ISSPLATQIPQAVGAAYAAKRANANRVVICYFGEGAASEGDAHAGFNFAA
TLECPIIFFCRNNGYAISTPTSEQYRGDGIAARGPGYGIMSIRVDGNDVF
AVYNATKEARRRAVAENQPFLIEAMTYRDHPISRLRHYLLSQGWWDEEQE
KAWRKQSRRKVMEAFEQAERKPKPNPNLLFSDVYQEMPAQLRKQQESLAR
HLQTYGEHYPLDHFDK
Ligand information
Ligand IDTPP
InChIInChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1
InChIKeyAYEKOFBPNLCAJY-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N
FormulaC12 H19 N4 O7 P2 S
NameTHIAMINE DIPHOSPHATE
ChEMBLCHEMBL1236376
DrugBank
ZINCZINC000008215517
PDB chain1olu Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1olu Roles of His291-Alpha and His146-Beta' in the Reductive Acylation Reaction Catalyzed by Human Branched-Chain Alpha-Ketoacid Dehydrogenase: Refined Phosphorylation Loop Structure in the Active Site.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		R114 L164 G192 E193 G194 A195 N222 A225 I226
Binding residue
(residue number reindexed from 1)		R105 L155 G183 E184 G185 A186 N213 A216 I217
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E76 S162 R287
Catalytic site (residue number reindexed from 1) E67 S153 R278
Enzyme Commision number 1.2.4.4: 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
Gene Ontology
Molecular Function
GO:0003863 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016624 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
GO:0016831 carboxy-lyase activity
GO:0046872 metal ion binding
GO:0047101 branched-chain alpha-keto acid dehydrogenase activity
Biological Process
GO:0009083 branched-chain amino acid catabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0045252 oxoglutarate dehydrogenase complex
GO:0160157 branched-chain alpha-ketoacid dehydrogenase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1olu, PDBe:1olu, PDBj:1olu
PDBsum1olu
PubMed12902323
UniProtP12694|ODBA_HUMAN 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (Gene Name=BCKDHA)

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