Structure of PDB 2b5w Chain A Binding Site BS03
Receptor Information
>2b5w Chain A (length=357) Species:
2252
(Haloferax mediterranei) [
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MKAIAVKRGEDRPVVIEKPRPEPESGEALVRTLRVGVCGTDHEVIAGGHG
GFPEGEDHLVLGHEAVGVVVDPNDTELEEGDIVVPTVRRPPASGTNEYFE
RDQPDMAPDGMYFERGIVGAHGYMSEFFTSPEKYLVRIPRSQAELGFLIE
PISITEKALEHAYASRSAFDWDPSSAFVLGNGSLGLLTLAMLKVDDKGYE
NLYCLGRRDRPDPTIDIIEELDATYVDSRQTPVEDVPDVYEQMDFIYEAT
GFPKHAIQSVQALAPNGVGALLGVPSDWAFEVDAGAFHREMVLHNKALVG
SVNSHVEHFEAATVTFTKLPKWFLEDLVTGVHPLSEFEAAFDDDDTTIKT
AIEFSTV
Ligand information
Ligand ID
K
InChI
InChI=1S/K/q+1
InChIKey
NPYPAHLBTDXSSS-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0
[K+]
Formula
K
Name
POTASSIUM ION
ChEMBL
CHEMBL1233793
DrugBank
DB01345
ZINC
PDB chain
2b5w Chain A Residue 902 [
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Receptor-Ligand Complex Structure
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PDB
2b5w
Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei.
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
D172 P173 S174 K197 G198 Y199
Binding residue
(residue number reindexed from 1)
D172 P173 S174 K197 G198 Y199
Annotation score
1
Enzymatic activity
Enzyme Commision number
1.1.1.47
: glucose 1-dehydrogenase [NAD(P)(+)].
Gene Ontology
Molecular Function
GO:0000166
nucleotide binding
GO:0005536
D-glucose binding
GO:0008270
zinc ion binding
GO:0016491
oxidoreductase activity
GO:0042802
identical protein binding
GO:0042803
protein homodimerization activity
GO:0046872
metal ion binding
GO:0047934
glucose 1-dehydrogenase (NAD+) activity
GO:0047935
glucose 1-dehydrogenase (NADP+) activity
GO:0047936
glucose 1-dehydrogenase [NAD(P)+] activity
GO:0070401
NADP+ binding
GO:0070403
NAD+ binding
Biological Process
GO:0019595
non-phosphorylated glucose catabolic process
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:2b5w
,
PDBe:2b5w
,
PDBj:2b5w
PDBsum
2b5w
PubMed
16551747
UniProt
Q977U7
|GLCDH_HALMT Glucose 1-dehydrogenase (Gene Name=gdh)
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