Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 Å

Structure

Volumn 8, Issue 11, 2000, Pages 1137-1146

  Devedjiev, Yancho ^a   Dauter, Zbigniew ^b   Kuznetsov, Sergey R ^c   Jones, Teresa L Z ^c   Derewenda, Zygmunt S ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b BROOKHAVEN NATIONAL LABORATORY   (United States)

^c NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

Anomalous diffraction; SAD; Serine hydrolase; hydrolase

Indexed keywords

ASPARTIC ACID; BROMIDE; CARBOXYLESTERASE; CRYOPROTECTIVE AGENT; DIMER; HISTIDINE; HYDROLASE; PALMITOYL PROTEIN THIOESTERASE; REGULATOR PROTEIN; SERINE;

ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HUMAN; NONHUMAN; PRIORITY JOURNAL; X RAY DIFFRACTION;

ACYLATION; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; EVOLUTION, MOLECULAR; HETEROTRIMERIC GTP-BINDING PROTEINS; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROLASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PALMITIC ACID; PROTEIN CONFORMATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; STRUCTURE-ACTIVITY RELATIONSHIP; THIOLESTER HYDROLASES;

EID: 0034435875     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00529-3     Document Type: Article

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