Structure of PDB 1jqb Chain D

Receptor sequence
>1jqbD (length=351) Species: 1520 (Clostridium beijerinckii) [Search protein sequence]
MKGFAMLGINKLGWIEKERPVAGSYDAIVRPLAVSPCTSDIHTVFEGALG
DRKNMILGHEAVGEVVEVGSEVKDFKPGDRVIVPCTTPDWRSLEVQAGFQ
QHSNGMLAGWKFSNFKDGVFGEYFHVNDADMNLAILPKDMPLENAVMITD
MMTTGFHGAELADIEMGSSVVVIGIGAVGLMGIAGAKLRGAGRIIGVGSR
PICVEAAKFYGATDILNYKNGHIEDQVMKLTNGKGVDRVIMAGGGSETLS
QAVKMVKPGGIISNINYHGSGDALLIPRVEWGCGMAHKTIKGGLCPGGRL
RAERLRDMVVYNRVDLSKLVTHVYHGFDHIEEALLLMKDKPKDLIKAVVI
L
3D structure
PDB1jqb Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging
ChainD
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C4037 T4038 S4039 H4042 H4059 E4060 D4089 S4092 V4095 S4103 D4150 T4154 K4346
Catalytic site (residue number reindexed from 1) C37 T38 S39 H42 H59 E60 D89 S92 V95 S103 D150 T154 K346
Enzyme Commision number 1.1.1.80: isopropanol dehydrogenase (NADP(+)).
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 D C4037 H4059 D4150 C37 H59 D150
Gene Ontology
Molecular Function
GO:0008270 zinc ion binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050009 isopropanol dehydrogenase (NADP+) activity

View graph for
Molecular Function
External links
PDB RCSB:1jqb, PDBe:1jqb, PDBj:1jqb
PDBsum1jqb
PubMed12381840
UniProtP25984|ADH_CLOBE NADP-dependent isopropanol dehydrogenase (Gene Name=adh)

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