Structure of PDB 2pnr Chain B Binding Site BS01

Receptor Information
>2pnr Chain B (length=341) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KQIERYSRFSPSPLSIKQFLDFGRDNACEKTSYMFLRKELPVRLANTMRE
VNLLPDNLLNRPSVGLVQSWYMQSFLELLEYENKSPEDPQVLDNFLQVLI
KVRNRHNDVVPTMAQGVIEYKEKSTNIQYFLDRFYTNRISFRMLINQHTL
LFGGDTNPVHPKHIGSIDPTCNVADVVKDAYETAKMLCEQYYLVAPELEV
EEFNAKAPDKPIQVVYVPSHLFHMLFELFKNSMRATVELYEDYPAVKTLV
TLGKEDLSIKISDLGGGVPLRKIDRLFNYMGLPISRLYARYFQGDLKLYS
MEGVGTDAVIYLKALSSESFERLPVFNKSAWRHYKTADDWS
Ligand information
Ligand IDRED
InChIInChI=1S/C8H16O2S2/c9-8(10)4-2-1-3-7(12)5-6-11/h7,11-12H,1-6H2,(H,9,10)/t7-/m1/s1
InChIKeyIZFHEQBZOYJLPK-SSDOTTSWSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CCC(=O)O)CC(CCS)S
OpenEye OEToolkits 1.5.0C(CCC(=O)O)C[C@H](CCS)S
ACDLabs 10.04O=C(O)CCCCC(S)CCS
CACTVS 3.341OC(=O)CCCC[C@@H](S)CCS
CACTVS 3.341OC(=O)CCCC[CH](S)CCS
FormulaC8 H16 O2 S2
NameDIHYDROLIPOIC ACID
ChEMBLCHEMBL1235647
DrugBankDB03760
ZINCZINC000003869601
PDB chain2pnr Chain C Residue 900 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2pnr Crystal Structure of an Asymmetric complex of Pyruvate Dehydrogenase Kinase 3 with Lipoyl domain 2 and its Biological Implications
Resolution2.5 Å
Binding residue
(original residue number in PDB)		Q31 F35 F48
Binding residue
(residue number reindexed from 1)		Q18 F22 F35
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H243 E247 K250 N251
Catalytic site (residue number reindexed from 1) H223 E227 K230 N231
Enzyme Commision number 2.7.11.2: [pyruvate dehydrogenase (acetyl-transferring)] kinase.
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0004740 pyruvate dehydrogenase (acetyl-transferring) kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0010510 regulation of acetyl-CoA biosynthetic process from pyruvate
GO:0010906 regulation of glucose metabolic process
GO:0016310 phosphorylation
GO:0018105 peptidyl-serine phosphorylation
GO:0035357 peroxisome proliferator activated receptor signaling pathway
GO:0071333 cellular response to glucose stimulus
GO:0071398 cellular response to fatty acid
GO:0097411 hypoxia-inducible factor-1alpha signaling pathway
GO:2000377 regulation of reactive oxygen species metabolic process
Cellular Component
GO:0005730 nucleolus
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:2pnr, PDBe:2pnr, PDBj:2pnr
PDBsum2pnr
PubMed17532006
UniProtQ15120|PDK3_HUMAN [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrial (Gene Name=PDK3)

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