Structure of PDB 3eya Chain A Binding Site BS03

Receptor Information
>3eya Chain A (length=527) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKQTVAAYIAKTLESAGVKRIWGVTGDSLNGLSDSLNRMGTIEWMSTRHE
EVAAFAAGAEAQLSGELAVCAGSCGPGNLHLINGLFDCHRNHVPVLAIAA
HIPSSEIGSGYFQETHPQELFRECSHYCELVSSPEQIPQVLAIAMRKAVL
NRGVSVVVLPGDVALKPAPEGATMHWYHAPQPVVTPEEEELRKLAQLLRY
SSNIALMCGSGCAGAHKELVEFAGKIKAPIVHALRGKEHVEYDNPYDVGM
TGLIGFSSGFHTMMNADTLVLLGTQFPYRAFYPTDAKIIQIDINPASIGA
HSKVDMALVGDIKSTLRALLPLVEEKADRKFLDKALEDYRDARKGLDDLA
KPSEKAIHPQYLAQQISHFAADDAIFTCDVGTPTVWAARYLKMNGKRRLL
GSFNHGSMANAMPQALGAQATEPERQVVAMCGDGGFSMLMGDFLSVVQMK
LPVKIVVFNNSVLGFVGTELHDTNFARIAEACGITGIRVEKASEVDEALQ
RAFSIDGPVLVDVVVAKEELAIPPQIK
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3eya Chain A Residue 613 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3eya Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		D433 N460 V462
Binding residue
(residue number reindexed from 1)		D433 N460 V462
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) V24 G26 D27 S28 L29 E50 S73 F112 Q113 G161 L253 A280 V380 G406 M408 D433 N460 V462 L463 F465 V466 K529
Catalytic site (residue number reindexed from 1) V24 G26 D27 S28 L29 E50 S73 F112 Q113 G161 L253 A280 V380 G406 M408 D433 N460 V462 L463 F465 V466 K517
Enzyme Commision number 1.2.5.1: pyruvate dehydrogenase (quinone).
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0008289 lipid binding
GO:0016491 oxidoreductase activity
GO:0030976 thiamine pyrophosphate binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0048039 ubiquinone binding
GO:0050660 flavin adenine dinucleotide binding
GO:0052737 pyruvate dehydrogenase (quinone) activity
Biological Process
GO:0006090 pyruvate metabolic process
GO:0019752 carboxylic acid metabolic process
GO:0042867 pyruvate catabolic process
Cellular Component
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3eya, PDBe:3eya, PDBj:3eya
PDBsum3eya
PubMed18988747
UniProtP07003|POXB_ECOLI Pyruvate dehydrogenase [ubiquinone] (Gene Name=poxB)

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