Structure of PDB 2b5w Chain A

Receptor sequence

>2b5wA (length=357) Species: 2252 (Haloferax mediterranei)

MKAIAVKRGEDRPVVIEKPRPEPESGEALVRTLRVGVCGTDHEVIAGGHG
GFPEGEDHLVLGHEAVGVVVDPNDTELEEGDIVVPTVRRPPASGTNEYFE
RDQPDMAPDGMYFERGIVGAHGYMSEFFTSPEKYLVRIPRSQAELGFLIE
PISITEKALEHAYASRSAFDWDPSSAFVLGNGSLGLLTLAMLKVDDKGYE
NLYCLGRRDRPDPTIDIIEELDATYVDSRQTPVEDVPDVYEQMDFIYEAT
GFPKHAIQSVQALAPNGVGALLGVPSDWAFEVDAGAFHREMVLHNKALVG
SVNSHVEHFEAATVTFTKLPKWFLEDLVTGVHPLSEFEAAFDDDDTTIKT
AIEFSTV

3D structure

• PDB: 2b5w Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei.
• Chain: A
• Resolution: 1.6 Å

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	ZN	A	C38 H63 E64	C38 H63 E64
BS02	K	A	D344 D345 T347	D344 D345 T347
BS03	K	A	D172 P173 S174 K197 G198 Y199	D172 P173 S174 K197 G198 Y199
BS04	K	A	E156 T315	E156 T315
BS05	NAP	A	G39 E43 I154 N181 G182 L184 G206 R207 R208 S228 A249 T250 F252 H255 L272 V302	G39 E43 I154 N181 G182 L184 G206 R207 R208 S228 A249 T250 F252 H255 L272 V302

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

External links

• PDB: RCSB:2b5w, PDBe:2b5w, PDBj:2b5w
• PDBsum: 2b5w
• PubMed: 16551747
• UniProt: Q977U7|GLCDH_HALMT Glucose 1-dehydrogenase (Gene Name=gdh)