Brand  (β version)

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hetatm:

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information
centroid:
interaction residue:

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Ligands
Code Name Link
ETF Trifluoroethanol
NAD Nicotinamide-adenine-dinucleotide
ZN Zinc ion
Code : 1A71
Header : OXIDOREDUCTASE
Title : TERNARY COMPLEX OF AN ACTIVE SITE DOUBLE MUTANT OF HORSE LIVER ALCOHOL DEHYDROGENASE, PHE93=>TRP, VAL203=>ALA WITH NAD AND TRIFLUOROETHANOL
Release Data : 1998-06-17
Compound :
mol_id molecule chains
1 LIVER ALCOHOL DEHYDROGENASE A,B
ec: 1.1.1.1
mutation: F93W, V203A
Source :
mol_id organism_scientific organism_common expression_system
1 Equus caballus  (taxid:9796) Horse Escherichia coli  (taxid:562)
organ: LIVER
cellular_location: CYTOPLASM
gene: LADH F93W V203A
expression_system_strain: XL1-BLUE
expression_system_cellular_location: CYTOPLASM
expression_system_vector_type: HELPER PHAGE
expression_system_vector: VCSM13
expression_system_plasmid: PHAGEMID PBPP-LADH
expression_system_gene: LADH F93W,V203A
Authors : Colby, T.D., Bahnson, B.J., Chin, J.K., Klinman, J.P., Goldstein, B.M.
Keywords : OXIDOREDUCTASE (NAD(A)-CHOH(D)), LIVER, ALCOHOL, DEHYDROGENASE, LADH, ACTIVE SITE MUTANT, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

Active site modifications in a double mutant of liver alcohol dehydrogenase: structural studies of two enzyme-ligand complexes.

Colby, T.D.,Bahnson, B.J.,Chin, J.K.  et al.
(1998)  Biochemistry  37 : 9295 - 9304

PubMed: 9649310
DOI: 10.1021/bi973184b

A Link between Protein Structure and Enzyme Catalyzed Hydrogen Tunneling

Bahnson, B.J.,Colby, T.D.,Chin, J.K.  et al.
(1997)  Proc.Natl.Acad.Sci.USA  94 : 12797

Chain : A, B
UniProt : P00327 (ADH1E_HORSE)
Reaction : An alcohol + NAD(+) = an aldehyde or ketone + NADH.