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Volumn 8, Issue 5, 2001, Pages 467-472
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The structure of adp-ribose pyrophosphatase reveals the structural basis for the versatility of the nudix family
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Author keywords
[No Author keywords available]
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Indexed keywords
ADENOSINE DIPHOSPHATE RIBOSE;
ADENOSINE DIPHOSPHATE RIBOSE PYROPHOSPHATASE;
ADENOSINE PHOSPHATE;
HELIX LOOP HELIX PROTEIN;
INORGANIC PYROPHOSPHATASE;
RIBOSE 5 PHOSPHATE;
UNCLASSIFIED DRUG;
ADENOSINE DIPHOSPHATE RIBOSYLATION;
ARTICLE;
CATALYSIS;
DIMERIZATION;
ENZYME REGULATION;
ENZYME SPECIFICITY;
ENZYME STRUCTURE;
HYDROLYSIS;
MOLECULAR RECOGNITION;
NONHUMAN;
NUCLEOTIDE METABOLISM;
PRIORITY JOURNAL;
PROTEIN FAMILY;
ADENOSINE DIPHOSPHATE RIBOSE;
AMINO ACID MOTIFS;
AMINO ACID SEQUENCE;
APOENZYMES;
BACTERIAL PROTEINS;
BINDING SITES;
CATIONS, DIVALENT;
CONSERVED SEQUENCE;
CRYSTALLOGRAPHY, X-RAY;
DIMERIZATION;
ENZYME ACTIVATION;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
HYDROLYSIS;
MAGNESIUM;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PHOSPHORIC MONOESTER HYDROLASES;
PROTEIN STRUCTURE, TERTIARY;
PYROPHOSPHATASES;
SEQUENCE ALIGNMENT;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
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EID: 0035026968
PISSN: 10728368
EISSN: None
Source Type: Journal
DOI: 10.1038/87647 Document Type: Article |
Times cited : (118)
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References (38)
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