Structure of PDB 2xgz Chain B

Receptor sequence

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

AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGANTGVHEALEMRD
GDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTA
NKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPF
LNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKR
YGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKIKIGLDCASS
EFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAE
DDWEAWSHFFKTAGIQIVADRLTVTNPKRIATAIEKKAADALLLKVNQIG
TLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKLL

3D structure

• PDB: 2xgz Engineering the Enolase Magnesium II Binding Site -Implications for its Evolution.
• Chain: B
• 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	B	D246 E295 D320	D246 E295 D320
BS02	PEP	B	E168 D246 E295 D320 K345 S375 K396	E168 D246 E295 D320 K345 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:2xgz, PDBe:2xgz, PDBj:2xgz
• PDBsum: 2xgz
• PubMed: 20690637
• UniProt: P00924|ENO1_YEAST Enolase 1 (Gene Name=ENO1)