Structure of PDB 2psn Chain D Binding Site BS01

Receptor Information
>2psn Chain D (length=431) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRD
NDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTE
NKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFN
VINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYG
KDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEF
FRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDW
GAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVT
ESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS
ERLAKYNQLLRIEEELGSKAKFAGRNFRNPL
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 chain2psn Chain D Residue 707 [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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PDB2psn Crystal Structure of Enolase1 alpha
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D244 E292 D317
Binding residue
(residue number reindexed from 1)		D244 E292 D317
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S39 H157 E166 E209 D244 E292 D317 K342 H370 K393
Catalytic site (residue number reindexed from 1) S39 H157 E166 E209 D244 E292 D317 K342 H370 K393
Enzyme Commision number 4.2.1.11: phosphopyruvate hydratase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding
GO:0001222 transcription corepressor binding
GO:0001227 DNA-binding transcription repressor activity, RNA polymerase II-specific
GO:0003677 DNA binding
GO:0003714 transcription corepressor activity
GO:0003723 RNA binding
GO:0004634 phosphopyruvate hydratase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0042803 protein homodimerization activity
GO:0045296 cadherin binding
GO:0046872 metal ion binding
GO:0051020 GTPase binding
Biological Process
GO:0000122 negative regulation of transcription by RNA polymerase II
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0009615 response to virus
GO:0010756 positive regulation of plasminogen activation
GO:0030308 negative regulation of cell growth
GO:0045892 negative regulation of DNA-templated transcription
GO:0045933 positive regulation of muscle contraction
GO:0061621 canonical glycolysis
GO:1903298 negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
GO:2001171 positive regulation of ATP biosynthetic process
Cellular Component
GO:0000015 phosphopyruvate hydratase complex
GO:0005615 extracellular space
GO:0005634 nucleus
GO:0005640 nuclear outer membrane
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005938 cell cortex
GO:0009986 cell surface
GO:0016020 membrane
GO:0031430 M band
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2psn, PDBe:2psn, PDBj:2psn
PDBsum2psn
PubMed
UniProtP06733|ENOA_HUMAN Alpha-enolase (Gene Name=ENO1)

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