Structure of PDB 5utm Chain D Binding Site BS02

Receptor Information
>5utm Chain D (length=334) Species: 1311 (Streptococcus agalactiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VVKVGINGFGRIGRLAFRRIQNVEGVEVTRINDLTDPNMLAHLLKYDTTQ
GRFDGTVEVKEGGFEVNGQFVKVSAEREPANIDWATDGVEIVLEATGFFA
SKEKAEQHIHENGAKKVVITAPGGNDVKTVVFNTNHDILDGTETVISGAS
CTTNCLAPMAKALQDNFGVKQGLMTTIHAYTGDQMILDGPHRGGDLRRAR
AGAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSVTELVATLE
KDVTVEEVNAAMKAAANDSYGYTEDPIVSSDIVGISYGSLFDATQTKVQT
VDGNTLVKVVSWYDNEMSYTSQLVRTLEYFAKIA
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 chain5utm Chain D Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5utm Mutant Structures of Streptococcus agalactiae GAPDH
Resolution1.77 Å
Binding residue
(original residue number in PDB)
I21 V24 V27
Binding residue
(residue number reindexed from 1)
I20 V23 V26
Annotation score1
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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Cellular Component
External links
PDB RCSB:5utm, PDBe:5utm, PDBj:5utm
PDBsum5utm
PubMed
UniProtQ9ALW2

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