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Ligands
Code Name Style Show Link
9ON (2~{S})-2-methylpentanedioic acid
NAD Nicotinamide-adenine-dinucleotide
ZN Zinc ion
Non-standard Residues
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Glycosylation
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Code : 5O9F   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Crystal structure of R. ruber ADH-A, mutant Y294F, W295A, Y54F, F43S, H39Y
Release Data : 2017-10-11
Compound :
mol_id molecule chains
1 Alcohol dehydrogenase A,B,C,D
mutation: Y294F, W295A, Y54F, F43S, H39Y
other_details: contains four mutations compared to wildtype enzyme C-terminally his-tagged
Source :
mol_id organism_scientific expression_system
1 Rhodococcus sp. M8  (taxid:1925550) Escherichia coli BL21  (taxid:511693)
gene: BKE56_025765
expression_system_variant: AI
expression_system_plasmid: pGT7ADHA-5H
Authors : Dobritzsch, D., Maurer, D., Hamnevik, E., Enugala, T.R., Widersten, M.
Keywords : alcohol dehydrogenase mutant variant, NADH-dependent, Zn2+-dependent, Rossmann fold, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.64 Å )
Citation :

Relaxation of nonproductive binding and increased rate of coenzyme release in an alcohol dehydrogenase increases turnover with a nonpreferred alcohol enantiomer.

Hamnevik, E.,Enugala, T.R.,Maurer, D.  et al.
(2017)  FEBS J.  284 : 3895 - 3914

PubMed: 28963762
DOI: 10.1111/febs.14279

Chain : A, B, C, D
UniProt : A0A1Q8I6M1
Reaction : -