Structure of PDB 1rwb Chain A

Receptor sequence
>1rwbA (length=261) Species: 1404 (Priestia megaterium) [Search protein sequence]
MYKDLEGKVVVITGSSTGLGKSMAIRFATEKAKVVVNYRSKEDEANSVLE
EIKKVGGEAIAVKGDVTVESDVINLVQSAIKEFGKLDVMINNAGLENPVS
SHEMSLSDWNKVIDTNLTGAFLGSREAIKYFVENDIKGTVINMSSVHEKI
PWPLFVHYAASKGGMKLMTKTLALEYAPKGIRVNNIGPGAINTPINAEKF
ADPEQRADVESMIPMGYIGEPEEIAAVAAWLASSEASYVTGITLFADGGM
TLYPSFQAGRG
3D structure
PDB1rwb Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G18 S145 Y158 K162
Catalytic site (residue number reindexed from 1) G18 S145 Y158 K162
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 NAD A G14 T17 G18 L19 R39 D65 V66 N92 A93 G94 T115 M143 S144 S145 Y158 K162 P188 G189 I191 T193 G14 T17 G18 L19 R39 D65 V66 N92 A93 G94 T115 M143 S144 S145 Y158 K162 P188 G189 I191 T193
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0047934 glucose 1-dehydrogenase (NAD+) activity
GO:0047935 glucose 1-dehydrogenase (NADP+) activity
GO:0047936 glucose 1-dehydrogenase [NAD(P)+] activity
Biological Process
GO:0030435 sporulation resulting in formation of a cellular spore

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Molecular Function
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Biological Process
External links
PDB RCSB:1rwb, PDBe:1rwb, PDBj:1rwb
PDBsum1rwb
PubMed15933031
UniProtP40288|DHG_PRIMG Glucose 1-dehydrogenase

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