Structure of PDB 7ri0 Chain A Binding Site BS01
Receptor Information
>7ri0 Chain A (length=430) Species:
330879
(Aspergillus fumigatus Af293) [
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PISKIHARSVYDSRGNPTVEVDVVTETGLHRAIVPSGASTGQHEAHELRD
GDKTQWGGKGVLKAVKNVNETIGPALIKENIDVKDQSKVDEFLNKLDGTA
NKSNLGANAILGVSLAVAKAGAAEKGVPLYAHISDLAGTKKPYVLPVPFQ
NVLNGGSHAGGRLAFQEFMIVPDSAPSFSEALRQGAEVYQKLKALAKKKY
GQSAGNVGDEGGVAPDIQTAEEALDLITEAIEQAGYTGKIKIAMDVASSE
FYKADVKKYDLDFKKWLTYEQLADLYKSLAAKYPIVSIEDPFAEDDWEAW
SYFYKTSDFQIVGDDLTVTNPGRIKKAIELKSCNALLLKVNQIGTLTESI
QAAKDSYADNWGVMVSHRSGETEDVTIADIAVGLRSGQIKTGAPCRSERL
AKLNQILRIEEELGENAVYAGSKFRTAVNL
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
7ri0 Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
7ri0
A structural model of the human plasminogen and Aspergillus fumigatus enolase complex.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
D246 E297 D322
Binding residue
(residue number reindexed from 1)
D245 E289 D314
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:0019863
IgE binding
GO:0046872
metal ion binding
Biological Process
GO:0006096
glycolytic process
Cellular Component
GO:0000015
phosphopyruvate hydratase complex
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:7ri0
,
PDBe:7ri0
,
PDBj:7ri0
PDBsum
7ri0
PubMed
35247004
UniProt
Q96X30
|ENO_ASPFU Enolase (Gene Name=enoA)
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