Structure of PDB 4z17 Chain B

Receptor sequence
>4z17B (length=420) Species: 324602 (Chloroflexus aurantiacus J-10-fl) [Search protein sequence]
STLIEAIVAREVLDSRGNPTIEVDVRLESGDVGRAIVPSGASTGAHEALE
LRDGDKSRYNGKGVLKAVQAVNEDIAEALIGFDAADQIALDQELIALDGT
PNKSKLGANAILGVSLAAAKAAAAAFGLPLYRYLGGVYAHVLPVPMMNIM
NGGQHAFQEFMIMPVGAESFREGLRWGAEIYHMLKKVIHDRGFSTTVGDE
GGFAPSLPTNDAPLQLIMEAIEKAGYRPGEQIVIALDPATTEIFEDGKYH
LKREGRSLSSAEMVDYWVDLVNRYPIISLEDGLAEDDWEGWALLRAKLGD
RVQLVGDDFLVTNVQRLQRAIEAKAANSILIKLNQIGSLTETLSAIQLAQ
RSGWTAVVSHRSGESEDVTIADLVVATNAGQIKTGAPARTDRIAKYNQLL
RIEEELGSAARYAGRSAFKV
3D structure
PDB4z17 Biochemical and Structural Characterization of Enolase from Chloroflexus aurantiacus: Evidence for a Thermophilic Origin.
ChainB
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S43 H156 E165 E206 D243 E286 D313 K338 H366 K389
Catalytic site (residue number reindexed from 1) S42 H155 E159 E200 D237 E280 D307 K332 H360 K383
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 D243 D313 D237 D307
BS02 PEP B K338 R367 S368 K389 K332 R361 S362 K383
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:4z17, PDBe:4z17, PDBj:4z17
PDBsum4z17
PubMed26082925
UniProtA9WCM4|ENO_CHLAA Enolase (Gene Name=eno)

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