Structure of PDB 1jqb Chain B

Receptor sequence
>1jqbB (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
ChainB
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D2089 S2092 V2095 S2103 D2150 T2154 K2346
Catalytic site (residue number reindexed from 1) 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 B C2037 H2059 E2060 D2150 C37 H59 E60 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)

[Back to BioLiP]