Structure of PDB 2akz Chain B Binding Site BS03

Receptor Information
>2akz Chain B (length=432) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRD
GDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTE
NKSKFGANAILGVSLAVCKAGAAERELPLYRHIAQLAGNSDLILPVPAFN
VINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG
KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIVIGMDVAASEF
YRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDDW
AAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVT
EAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS
ERLAKYNQLMRIEEELGDEARFAGHNFRNPSV
Ligand information
Ligand IDF
InChIInChI=1S/FH/h1H/p-1
InChIKeyKRHYYFGTRYWZRS-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[F-]
FormulaF
NameFLUORIDE ION
ChEMBL
DrugBankDB11257
ZINC
PDB chain2akz Chain B Residue 1445 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2akz Fluoride inhibition of enolase: crystal structure and thermodynamics
Resolution1.36 Å
Binding residue
(original residue number in PDB)		K1342 K1393
Binding residue
(residue number reindexed from 1)		K342 K393
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S1039 H1157 E1166 E1209 D1244 E1292 D1317 K1342 H1370 K1393
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:0004634 phosphopyruvate hydratase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0061621 canonical glycolysis
Cellular Component
GO:0000015 phosphopyruvate hydratase complex
GO:0001917 photoreceptor inner segment
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0043025 neuronal cell body
GO:0043204 perikaryon
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:2akz, PDBe:2akz, PDBj:2akz
PDBsum2akz
PubMed16411755
UniProtP09104|ENOG_HUMAN Gamma-enolase (Gene Name=ENO2)

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