Structure of PDB 4yws Chain A

Receptor sequence

>4ywsA (length=405) Species: 324602 (Chloroflexus aurantiacus J-10-fl)

STLIEAIVAREVLDSRGNPTIEVDVRLESGDVGRAIVPSGSTGAHEALEL
RDGDKSRYNGKGVLKAVQAVNEDIAEALIGFDAADQIALDQELIALDGTP
NKSKLGANAILGVSLAAAKAAAAAFGLPLYRYLGGVYAHVLPVPMMNIMN
GGQHATNFQEFMIMPVGAESFREGLRWGAEIYHMLKKVIHDRGFGGFAPS
LTNDAPLQLIMEAIEKAGYRPGEQIVIALDPATTEIFDGYLKREGRSSAE
MVDYWVDLVNRYPIISLEDGLAEDDWEGWALLRAKLGDRVQLVGDDFLVT
NVQRLQRAIEAKAANSILIKLNQIGSLTETLSAIQLAQRGWTAVVSHRSG
ESEDVTIADLVVATNAGQIKTGAPATDIAKYNQLLRIEEELGSAARYAGR
SAFKV

3D structure

• PDB: 4yws Biochemical and Structural Characterization of Enolase from Chloroflexus aurantiacus: Evidence for a Thermophilic Origin.
• Chain: A
• Resolution: 2.45 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H156 E165 D243 E286 D313 K338 H366 K389
• Catalytic site (residue number reindexed from 1): H154 E160 D230 E268 D295 K320 H347 K370
• 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	D243 E286 D313	D230 E268 D295

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

External links

• PDB: RCSB:4yws, PDBe:4yws, PDBj:4yws
• PDBsum: 4yws
• PubMed: 26082925
• UniProt: A9WCM4|ENO_CHLAA Enolase (Gene Name=eno)