1egb

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THEORETICAL MODEL OF THE BINDING DOMAIN OF A CELLOBIOHYDROLASE FROM CORIOLUS VERSICOLORTHEORETICAL MODEL OF THE BINDING DOMAIN OF A CELLOBIOHYDROLASE FROM CORIOLUS VERSICOLOR

Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed Molecular cloning and cDNA sequencing analysis were used to elucidate the primary structure of a cellulase-like structure from the white-rot fungus Coriolus versicolor. The cDNA of interest was isolated from a cDNA library obtained from C. versicolor mycelia grown on cellulase inducer medium. A pattern search showed that this cellulase belongs to the glycosyl hydrolases family 6. From the deduced amino acid sequence, models of the binding and catalytic domains were built by homology modelling. The constructed models present a typical cellulose-binding domain at the N-terminal region, a rich Pro, Ser, Thr linker peptide, and a catalytic domain at the C-terminus region. Primary structure deduction and molecular modelling from a cDNA of a cellobiohydrolase-like protein from the white-rot fungus Coriolus versicolor.,Novo C, Simoes F, Mendonca D, Matos J, Clemente A Int J Biol Macromol. 2001 Apr 12;28(4):285-92. PMID:11311718 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1egb Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image