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BioLiP

Structure of PDB 2xh4 Chain D

Receptor sequence
>2xh4D (length=414) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGGVLHAVKNVNDVI
APAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAA
AEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIA
PTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAE
EALDLIVDAIKAAGHDGKIKIGLDCASSEFFKDGKYDLDFKNNSDKSKWL
TGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADALT
VTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSH
RSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDNA
VFAGENFHHGDKLL
3D structure
PDB2xh4 Engineering the Enolase Magnesium II Binding Site -Implications for its Evolution.
ChainD
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H159 E168 E211 D246 E295 D320 K345 H373 K396
Catalytic site (residue number reindexed from 1) H137 E146 E189 D224 E272 D297 K322 H350 K373
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 D D246 E295 D320 D224 E272 D297
BS02 2PG D H159 Q167 E168 E211 D246 D320 K345 H373 R374 S375 K396 H137 Q145 E146 E189 D224 D297 K322 H350 R351 S352 K373
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

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Cellular Component
External links
PDB RCSB:2xh4, PDBe:2xh4, PDBj:2xh4
PDBsum2xh4
PubMed20690637
UniProtP00924|ENO1_YEAST Enolase 1 (Gene Name=ENO1)

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