Structure of PDB 1l8p Chain A

Receptor sequence
>1l8pA (length=436) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGAATGVHEALEMRD
GDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTA
NKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPF
LNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKR
YGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASS
EFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAE
DDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIG
TLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL
3D structure
PDB1l8p Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
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 PAH A G37 A38 E168 D246 D320 K345 R374 S375 K396 G37 A38 E168 D246 D320 K345 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:1l8p, PDBe:1l8p, PDBj:1l8p
PDBsum1l8p
PubMed12054465
UniProtP00924|ENO1_YEAST Enolase 1 (Gene Name=ENO1)

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