Structure of PDB 5enl Chain A

Receptor sequence

>5enlA (length=436) Species: 4932 (Saccharomyces cerevisiae)

AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRD
GDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVSDQKAVDDFLISLDGTA
NKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPF
LNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKR
YGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASS
EFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAE
DDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIG
TLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL

3D structure

• PDB: 5enl Inhibition of enolase: the crystal structures of enolase-Ca2(+)- 2-phosphoglycerate and enolase-Zn2(+)-phosphoglycolate complexes at 2.2-A resolution.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S39 H159 E168 E211 D246 E295 D320 K345 H373 K396
• Catalytic site (residue number reindexed from 1): S39 H159 E168 E211 D246 E295 D320 K345 H373 K396
• 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	CA	A	D246 E295 D320	D246 E295 D320
BS02	2PG	A	E168 E211 K345 H373 R374 S375	E168 E211 K345 H373 R374 S375

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004634 phosphopyruvate hydratase activity
• GO:0016829 lyase activity
• GO:0046872 metal ion binding
• GO:1904408 melatonin binding

Biological Process

• GO:0006096 glycolytic process
• GO:0032889 regulation of vacuole fusion, non-autophagic

Cellular Component

• GO:0000015 phosphopyruvate hydratase complex
• GO:0000324 fungal-type vacuole
• GO:0005737 cytoplasm
• GO:0005739 mitochondrion
• GO:0005829 cytosol
• GO:0005886 plasma membrane

External links

• PDB: RCSB:5enl, PDBe:5enl, PDBj:5enl
• PDBsum: 5enl
• PubMed: 2007121
• UniProt: P00924|ENO1_YEAST Enolase 1 (Gene Name=ENO1)