Structure of PDB 2akm Chain A

Receptor sequence
>2akmA (length=433) Species: 9606 (Homo sapiens) [Search protein sequence]
SIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRD
GDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTE
NKSKFGANAILGVSLAVCKAGAAERELPLYRHIAQLAGNSDLILPVPAFN
VINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYG
KDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIVIGMDVAASEF
YRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDDW
AAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVT
EAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRS
ERLAKYNQLMRIEEELGDEARFAGHNFRNPSVL
3D structure
PDB2akm Fluoride inhibition of enolase: crystal structure and thermodynamics
ChainA
Resolution1.92 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 MG A D244 E292 D317 D244 E292 D317
BS02 PO4 A A38 S39 H157 R371 S372 A38 S39 H157 R371 S372
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2akm, PDBe:2akm, PDBj:2akm
PDBsum2akm
PubMed16411755
UniProtP09104|ENOG_HUMAN Gamma-enolase (Gene Name=ENO2)

[Back to BioLiP]