Structure of PDB 2xh2 Chain A

Receptor sequence

>2xh2A (length=437) Species: 4932 (Saccharomyces cerevisiae)

AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGANTGVHEALEMRD
GDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTA
NKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPF
LNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKR
YGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKIKIGLDCASS
EFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAE
DDWEAWSHFFKTAGIQIVADALTVTNPKRIATAIEKKAADALLLKVNQIG
TLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKLL

3D structure

• PDB: 2xh2 Engineering the Enolase Magnesium II Binding Site -Implications for its Evolution.
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N39 H159 E168 E211 D246 E295 D320 K345 H373 K396
• Catalytic site (residue number reindexed from 1): N39 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	MG	A	D246 E295 D320	D246 E295 D320
BS02	2PG	A	G37 A38 E211 D246 D320 K345 H373 R374 S375 K396	G37 A38 E211 D246 D320 K345 H373 R374 S375 K396

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:2xh2, PDBe:2xh2, PDBj:2xh2
• PDBsum: 2xh2
• PubMed: 20690637
• UniProt: P00924|ENO1_YEAST Enolase 1 (Gene Name=ENO1)