Structure of PDB 2akz Chain A Binding Site BS03
Receptor Information
>2akz Chain A (length=435) Species:
9606
(Homo sapiens) [
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SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRD
GDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTE
NKSKFGANAILGVSLAVCKAGAAERELPLYRHIAQLAGNSDLILPVPAFN
VINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG
KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIVIGMDVAASEF
YRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDDW
AAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVT
EAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS
ERLAKYNQLMRIEEELGDEARFAGHNFRNPSVLHH
Ligand information
Ligand ID
F
InChI
InChI=1S/FH/h1H/p-1
InChIKey
KRHYYFGTRYWZRS-UHFFFAOYSA-M
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[F-]
Formula
F
Name
FLUORIDE ION
ChEMBL
DrugBank
DB11257
ZINC
PDB chain
2akz Chain A Residue 445 [
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Receptor-Ligand Complex Structure
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PDB
2akz
Fluoride inhibition of enolase: crystal structure and thermodynamics
Resolution
1.36 Å
Binding residue
(original residue number in PDB)
K342 K393
Binding residue
(residue number reindexed from 1)
K342 K393
Annotation score
1
Enzymatic activity
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
PDBsum
2akz
PubMed
16411755
UniProt
P09104
|ENOG_HUMAN Gamma-enolase (Gene Name=ENO2)
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