Structure of PDB 2vwh Chain A

Receptor sequence
>2vwhA (length=357) Species: 2252 (Haloferax mediterranei) [Search protein sequence]
MKAIAVKRGEDRPVVIEKPRPEPESGEALVRTLRVGVDGTDHEVIAGGHG
GFPEGEDHLVLGHEAVGVVVDPNDTELEEGDIVVPTVRRPPASGTNEYFE
RDQPDMAPDGMYFERGIVGAHGYMSEFFTSPEKYLVRIPRSQAELGFLIE
PISITEKALEHAYASRSAFDWDPSSAFVLGNGSLGLLTLAMLKVDDKGYE
NLYCLGRRDRPDPTIDIIEELDATYVDSRQTPVEDVPDVYEQMDFIYEAT
GFPKHAIQSVQALAPNGVGALLGVPSDWAFEVDAGAFHREMVLHNKALVG
SVNSHVEHFEAATVTFTKLPKWFLEDLVTGVHPLSEFEAAFDDDDTTIKT
AIEFSTV
3D structure
PDB2vwh Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily.
ChainA
Resolution2.03 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.1.1.47: glucose 1-dehydrogenase [NAD(P)(+)].
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 NAP A G39 T40 N181 G182 L184 G206 R207 R208 S228 H255 L272 V302 G39 T40 N181 G182 L184 G206 R207 R208 S228 H255 L272 V302
BS02 BGC A T40 H63 E114 E150 V302 N303 T40 H63 E114 E150 V302 N303
BS03 ZN A D38 H63 D38 H63
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

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Molecular Function

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Biological Process
External links
PDB RCSB:2vwh, PDBe:2vwh, PDBj:2vwh
PDBsum2vwh
PubMed19131516
UniProtQ977U7|GLCDH_HALMT Glucose 1-dehydrogenase (Gene Name=gdh)

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