Structure of PDB 2b83 Chain C

Receptor sequence
>2b83C (length=351) Species: 1520 (Clostridium beijerinckii) [Search protein sequence]
MKGFAMLGINKLGWIEKERPVAGSYDAIVRPLAVSPCTSDIHTVFEGALG
DRKNMILGHEAVGEVVEVGSEVKDFKPGDRVIVPCTTPDWRSLEVQAGFP
QHSNGMLAGWKFSNFKDGVFGEYFHVNDADMNLAILPKDMPLENAVMITD
MMTTGFHGAELADIQMGSSVVVIGIGAVGLMGIAGAKLRGAGRIIGVGSR
PICVEAAKFYGATDILNYKNGHIVDQVMKLTNGKGVDRVIMAGGGSETLS
QAVSMVKPGGIISNINYHGSGDALLIPRVEWGCGMAHKTIKGGLCPGGRL
RAEMLRDMVVYNRVDLSKLVTHVYHGFDHIEEALLLMKDKPKDLIKAVVI
L
3D structure
PDB2b83 A single proline substitution is critical for the thermostabilization of Clostridium beijerinckii alcohol dehydrogenase.
ChainC
Resolution2.25 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) C37 T38 S39 H42 H59 E60 D89 S92 V95 S103 D150 T154 K346
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 C C37 H59 E60 D150 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:2b83, PDBe:2b83, PDBj:2b83
PDBsum2b83
PubMed17063493
UniProtP25984|ADH_CLOBE NADP-dependent isopropanol dehydrogenase (Gene Name=adh)

[Back to BioLiP]