Structure of PDB 1iyx Chain B

Receptor sequence
>1iyxB (length=431) Species: 1354 (Enterococcus hirae) [Search protein sequence]
SIITDVYAREILDSRGNPTIEVEVYTESGAFGRGMVPSGASTGEYEAVEL
RDGDKARYGGKGVTKAVDNVNNIIAEAIIGYDVRDQMAIDKAMIALDGTP
NKGKLGANAILGVSIAVARAAADYLEVPLYHYLGGFNTKVLPTPMMNIIN
GGSHADNSIDFQEFMIMPVGAPTFKEALRMGAEVFHALAAILKSRGLATS
VGDEGGFAPNLGSNEEGFEVIIEAIEKAGYVPGKDVVLAMDAASSEFYDK
EKGVYVLADSGEGEKTTDEMIKFYEELVSKYPIISIEDGLDENDWDGFKK
LTDVLGDKVQLVGDDLFVTNTQKLSEGIEKGIANSILIKVNQIGTLTETF
EAIEMAKEAGYTAVVSHRSGETEDSTISDIAVATNAGQIKTGSLSRTDRI
AKYNQLLRIEDQLGEVAEYKGLKSFYNLKAA
3D structure
PDB1iyx Crystal Structure of Enterococcus hirae Enolase at 2.8 A Resolution
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S41 H154 E163 E204 D241 E287 D314 K339 H367 K390
Catalytic site (residue number reindexed from 1) S41 H154 E163 E204 D241 E287 D314 K339 H367 K390
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 B D241 D314 D241 D314
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004634 phosphopyruvate hydratase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
Cellular Component
GO:0000015 phosphopyruvate hydratase complex
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0009986 cell surface

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Molecular Function
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Cellular Component
External links
PDB RCSB:1iyx, PDBe:1iyx, PDBj:1iyx
PDBsum1iyx
PubMed12869539
UniProtQ8GR70|ENO_ENTHR Enolase (Gene Name=eno)

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