Structure of PDB 6cfo Chain C Binding Site BS01

Receptor Information
>6cfo Chain C (length=362) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKA
DQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRG
LSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIA
LACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYG
MGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKG
PILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSN
LASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVR
GANQWIKFKSVS
Ligand information
Ligand IDA5X
InChIInChI=1S/C14H23N4O10P3S/c1-8-11(4-5-27-31(25,26)28-30(22,23)24)32-13(14(3,19)29(20)21)18(8)7-10-6-16-9(2)17-12(10)15/h6,19,29H,4-5,7H2,1-3H3,(H5-,15,16,17,20,21,22,23,24,25,26)/p+1/t14-/m0/s1
InChIKeyCAOFPOCACDCAFN-AWEZNQCLSA-O
SMILES
SoftwareSMILES
ACDLabs 12.01OP(=O)(O)OP(OCCc1c([n+](c(s1)C(P(O)=O)(C)O)Cc2cnc(nc2N)C)C)(O)=O
CACTVS 3.385Cc1ncc(C[n+]2c(C)c(CCO[P](O)(=O)O[P](O)(O)=O)sc2[C@@](C)(O)[PH](O)=O)c(N)n1
CACTVS 3.385Cc1ncc(C[n+]2c(C)c(CCO[P](O)(=O)O[P](O)(O)=O)sc2[C](C)(O)[PH](O)=O)c(N)n1
OpenEye OEToolkits 2.0.6Cc1c(sc([n+]1Cc2cnc(nc2N)C)C(C)(O)P(=O)O)CCOP(=O)(O)OP(=O)(O)O
OpenEye OEToolkits 2.0.6Cc1c(sc([n+]1Cc2cnc(nc2N)C)[C@@](C)(O)P(=O)O)CCOP(=O)(O)OP(=O)(O)O
FormulaC14 H24 N4 O10 P3 S
Name3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-2-{(1S)-1-hydroxy-1-[(R)-hydroxy(oxo)-lambda~5~-phosphanyl]ethyl}-5-(2-{[(S)-hydroxy(phosphonooxy)phosphoryl]oxy}ethyl)-4-methyl-1,3-thiazol-3-ium
ChEMBL
DrugBank
ZINC
PDB chain6cfo Chain C Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6cfo Pyruvate dehydrogenase complex deficiency is linked to regulatory loop disorder in the alpha V138M variant of human pyruvate dehydrogenase.
Resolution2.7 Å
Binding residue
(original residue number in PDB)		F61 Y89 R90 G136 V138 G166 D167 G168 A169 N196 Y198 G199 H263
Binding residue
(residue number reindexed from 1)		F62 Y90 R91 G137 V139 G167 D168 G169 A170 N197 Y199 G200 H264
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q51 G136 R259 H263 S264 Y272
Catalytic site (residue number reindexed from 1) Q52 G137 R260 H264 S265 Y273
Enzyme Commision number 1.2.4.1: pyruvate dehydrogenase (acetyl-transferring).
Gene Ontology
Molecular Function
GO:0004738 pyruvate dehydrogenase activity
GO:0004739 pyruvate dehydrogenase (acetyl-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:0034604 pyruvate dehydrogenase (NAD+) activity
GO:0046872 metal ion binding
Biological Process
GO:0006006 glucose metabolic process
GO:0006086 acetyl-CoA biosynthetic process from pyruvate
GO:0006090 pyruvate metabolic process
GO:0006099 tricarboxylic acid cycle
Cellular Component
GO:0005634 nucleus
GO:0005730 nucleolus
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0043231 intracellular membrane-bounded organelle
GO:0045254 pyruvate dehydrogenase complex
GO:1902494 catalytic complex

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Molecular Function
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Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6cfo, PDBe:6cfo, PDBj:6cfo
PDBsum6cfo
PubMed29970614
UniProtP08559|ODPA_HUMAN Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (Gene Name=PDHA1)

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