The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18

Journal of Molecular Biology

Volumn 262, Issue 2, 1996, Pages 243-257

  Terwisscha Van Scheltinga, Anke C ^a   Hennig, Michael ^b,c   Dijkstra, Bauke W ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b UNIVERSITY OF BASEL   (Switzerland)

^c F HOFFMANN LA ROCHE LTD   (Switzerland)

Author keywords

cis peptide; Crystal contacts; Glycosyl hydrolase; TIM barrel; X ray structure comparison

Indexed keywords

CHITINASE; GLYCOSIDASE; LYSOZYME; BETA N ACETYLHEXOSAMINIDASE; CONCANAVALIN B PROTEIN, CANAVALIA ENSIFORMIS; GLOBULIN; GLYCOSYLCERAMIDASE; HEVAMINE; N ACETYL BETA GLUCOSAMINIDASE; NARBONIN; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SPECIFICITY; GENETIC CONSERVATION; NONHUMAN; PLANT; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN TERTIARY STRUCTURE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ENZYMOLOGY; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS);

AMINO ACID SEQUENCE; BINDING SITES; CHITINASE; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; GLOBULINS; GLYCOSYLCERAMIDASE; HEXOSAMINIDASES; MANNOSYL-GLYCOPROTEIN ENDO-BETA-N-ACETYLGLUCOSAMINIDASE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MURAMIDASE; PLANT PROTEINS; PLANTS; PROTEIN CONFORMATION; VEGETABLE PROTEINS;

EID: 0030595119     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0510     Document Type: Article

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