Structure of PDB 5utm Chain D Binding Site BS02
Receptor Information
>5utm Chain D (length=334) Species:
1311
(Streptococcus agalactiae) [
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VVKVGINGFGRIGRLAFRRIQNVEGVEVTRINDLTDPNMLAHLLKYDTTQ
GRFDGTVEVKEGGFEVNGQFVKVSAEREPANIDWATDGVEIVLEATGFFA
SKEKAEQHIHENGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGAS
CTTNCLAPMAKALQDNFGVKQGLMTTIHAYTGDQMILDGPHRGGDLRRAR
AGAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVATLE
KDVTVEEVNAAMKAAANDSYGYTEDPIVSSDIVGISYGSLFDATQTKVQT
VDGNTLVKVVSWYDNEMSYTSQLVRTLEYFAKIA
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
5utm Chain D Residue 402 [
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Receptor-Ligand Complex Structure
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PDB
5utm
Mutant Structures of Streptococcus agalactiae GAPDH
Resolution
1.77 Å
Binding residue
(original residue number in PDB)
I21 V24 V27
Binding residue
(residue number reindexed from 1)
I20 V23 V26
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.2.1.-
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0004365
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
GO:0016491
oxidoreductase activity
GO:0016620
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0042802
identical protein binding
GO:0046872
metal ion binding
GO:0050661
NADP binding
GO:0051287
NAD binding
Biological Process
GO:0006006
glucose metabolic process
GO:0006096
glycolytic process
Cellular Component
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:5utm
,
PDBe:5utm
,
PDBj:5utm
PDBsum
5utm
PubMed
UniProt
Q9ALW2
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