Structure of PDB 1l8p Chain A Binding Site BS01
Receptor Information
>1l8p Chain A (length=436) Species:
4932
(Saccharomyces cerevisiae) [
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AVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGAATGVHEALEMRD
GDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTA
NKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPF
LNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKR
YGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASS
EFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAE
DDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIG
TLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAP
ARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
1l8p Chain A Residue 438 [
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Receptor-Ligand Complex Structure
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PDB
1l8p
Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
D246 E295 D320
Binding residue
(residue number reindexed from 1)
D246 E295 D320
Annotation score
1
Enzymatic activity
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
PDBsum
1l8p
PubMed
12054465
UniProt
P00924
|ENO1_YEAST Enolase 1 (Gene Name=ENO1)
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