Structure of PDB 5boe Chain B

Receptor sequence
>5boeB (length=433) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
MPIITDVYAREVLDSRGNPTVEVEVLTESGAFGRALVPSGASTGEHEAVE
LRDGDKSRYLGKGVTKAVENVNEIIAPEIIEGEFSVLDQVSIDKMMIALD
GTPNKGKLGANAILGVSIAVARAAADLLGQPLYKYLGGFNGKQLPVPMMN
IVNGGSHSDAPIAFQEFMILPVGATTFKESLRWGTEIFHNLKSILSKRGL
ETAVGDEGGFAPKFEGTEDAVETIIQAIEAAGYKPGEEVFLGFDCASSEF
YENGVYDYSKFEGEHGAKRTAAEQVDYLEQLVDKYPIITIEDGMDENDWD
GWKQLTERIGDRVQLVGDDLFVTNTEILAKGIENGIGNSILIKVNQIGTL
TETFDAIEMAQKAGYTAVVSHRSGETEDTTIADIAVATNAGQIKTGSLSR
TDRIAKYNQLLRIEDELFETAKYDGIKSFYNLD
3D structure
PDB5boe Octameric structure of Staphylococcus aureus enolase in complex with phosphoenolpyruvate
ChainB
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S42 H157 E166 E207 D244 E291 D318 K343 H371 K394
Catalytic site (residue number reindexed from 1) S42 H157 E166 E207 D244 E291 D318 K343 H371 K394
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 PEP B K343 H371 R372 S373 K394 K343 H371 R372 S373 K394
BS02 MG B D244 E291 D318 D244 E291 D318
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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Biological Process
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Cellular Component
External links
PDB RCSB:5boe, PDBe:5boe, PDBj:5boe
PDBsum5boe
PubMed26627653
UniProtO69174|ENO_STAAU Enolase (Gene Name=eno)

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