Structure of PDB 1l8p Chain B Binding Site BS01

Receptor Information
>1l8p Chain B (length=436) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGAATGVHEALEMRD
GDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTA
NKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPF
LNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKR
YGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASS
EFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAE
DDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIG
TLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1l8p Chain B Residue 938 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1l8p Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		D746 E795 D820
Binding residue
(residue number reindexed from 1)		D246 E295 D320
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) A539 H659 E668 E711 D746 E795 D820 K845 H873 K896
Catalytic site (residue number reindexed from 1) A39 H159 E168 E211 D246 E295 D320 K345 H373 K396
Enzyme Commision number 4.2.1.11: phosphopyruvate hydratase.
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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