Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution
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The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework.Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutionsCrystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolutionUse of a non-rigid region in T4 lysozyme to design an adaptable metal-binding siteStructure of Trypanosoma cruzi glycosomal glyceraldehyde-3-phosphate dehydrogenase complexed with chalepin, a natural product inhibitor, at 1.95 A resolutionCrystal Structures of the Quinone Oxidoreductase from Thermus thermophilus HB8 and Its Complex with NADPH: Implication for NADPH and Substrate RecognitionStructure of formaldehyde dehydrogenase fromPseudomonas aeruginosa: the binary complex with the cofactor NAD+Effects of Cavities at the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase on Structure, Dynamics and CatalysisEnantioselective oxidation of galactitol 1-phosphate by galactitol-1-phosphate 5-dehydrogenase from Escherichia coliX-ray crystallographic investigation of substrate binding to carboxypeptidase A at subzero temperatureRefinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartateStructure of dehydroquinate synthase reveals an active site capable of multistep catalysisExploring the conformational equilibrium of E. coli thioredoxin reductase: characterization of two catalytically important states by ultrafast flavin fluorescence spectroscopyEnantioselective affinity labelling of horse liver alcohol dehydrogenase. Correlation of inactivation kinetics with the three-dimensional structure of the enzymeA novel subtype of class II alcohol dehydrogenase in rodents. Unique Pro(47) and Ser(182) modulates hydride transfer in the mouse enzymeCrystal structure of rat liver dihydropteridine reductaseOverview of protein structural and functional folds.Protein structure and neutral theory of evolution.Minimal functional sites allow a classification of zinc sites in proteins.Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivativesStructure of the complex of active site metal-depleted horse liver alcohol dehydrogenase and NADH.Structural trees for protein superfamilies.Molecular characterization of benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II of Acinetobacter calcoaceticus.Database of ligand-induced domain movements in enzymesConformational changes and catalysis by alcohol dehydrogenase.areABC genes determine the catabolism of aryl esters in Acinetobacter sp. Strain ADP1.Horse Liver Alcohol Dehydrogenase: Zinc Coordination and Catalysis.A Structural-informatics approach for tracing beta-sheets: building pseudo-C(alpha) traces for beta-strands in intermediate-resolution density maps.Yeast alcohol dehydrogenase structure and catalysis.Modulation of functionally significant conformational equilibria in adenylate kinase by high concentrations of trimethylamine oxide attributed to volume exclusionThe NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.Role of conserved glycine in zinc-dependent medium chain dehydrogenase/reductase superfamilyDetermination of the absolute configuration of (+)-neopentyl-1-d alcohol by neutron and x-ray diffraction analysis.Human liver alcohol dehydrogenase: amino acid substitution in the beta 2 beta 2 Oriental isozyme explains functional properties, establishes an active site structure, and parallels mutational exchanges in the yeast enzymeCoordination environment of the active-site metal ion of liver alcohol dehydrogenaseIdentification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases.Isolation of a glucan-binding domain of glucosyltransferase (1,6-alpha-glucan synthase) from Streptococcus sobrinusBinding energy, conformational change, and the mechanism of transmembrane solute movementsCloning and expression of an NADP(+)-dependent alcohol dehydrogenase gene of Entamoeba histolytica.Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenase.
P2860
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P2860
Structure of a triclinic ternary complex of horse liver alcohol dehydrogenase at 2.9 A resolution
description
1981 nî lūn-bûn
@nan
1981 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1981 թվականի մարտին հրատարակված գիտական հոդված
@hy
1981年の論文
@ja
1981年学术文章
@wuu
1981年学术文章
@zh-cn
1981年学术文章
@zh-hans
1981年学术文章
@zh-my
1981年学术文章
@zh-sg
1981年學術文章
@yue
name
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@ast
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@en
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@nl
type
label
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@ast
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@en
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@nl
prefLabel
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@ast
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@en
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@nl
P2093
P1476
Structure of a triclinic terna ...... ydrogenase at 2.9 A resolution
@en
P2093
P304
P356
10.1016/0022-2836(81)90047-4
P407
P577
1981-03-15T00:00:00Z