Structure of PDB 2al2 Chain A

Receptor sequence
>2al2A (length=436) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRD
GDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTA
NKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPF
LNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKR
YGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASS
EFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAE
DDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLAVNQIG
TLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL
3D structure
PDB2al2 Structure and catalytic properties of an engineered heterodimer of enolase composed of one active and one inactive subunit
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S39 H159 E168 E211 D246 E295 D320 A345 H373 K396
Catalytic site (residue number reindexed from 1) S39 H159 E168 E211 D246 E295 D320 A345 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 PEP A G37 A38 S39 H159 Q167 E168 D246 D320 R374 S375 K396 G37 A38 S39 H159 Q167 E168 D246 D320 R374 S375 K396
BS03 2PG A A38 S39 H159 Q167 E168 E211 D246 D320 R374 S375 K396 A38 S39 H159 Q167 E168 E211 D246 D320 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2al2, PDBe:2al2, PDBj:2al2
PDBsum2al2
PubMed16309698
UniProtP00924|ENO1_YEAST Enolase 1 (Gene Name=ENO1)

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