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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>

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PDB ID1azj  sequence information (FASTA format)   
DescriptorCELLOBIOHYDROLASE I
TitleTHREE-DIMENSIONAL STRUCTURES OF THREE ENGINEERED CELLULOSE-BINDING DOMAINS OF CELLOBIOHYDROLASE I FROM TRICHODERMA REESEI, NMR, 18 STRUCTURES
Functional KeywordsCELLULASE, NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY, PROTEIN-CARBOHYDRATE INTERACTION, CELLULOSE DEGRADATION, HYDROLASE, GLYCOSIDASE
Biological sourceHypocrea jecorina
Cellular location [UNP - P62694] Secreted
Total number of polymer chains1
Total molecular weight3654 (the details in Structural Details Page)
AuthorsMattinen, M.-L. (deposition date : 1997-11-18, release date : 1998-04-29)
Primary citationMattinen, M.L. , Kontteli, M. , Kerovuo, J. , Linder, M. , Annila, A. , Lindeberg, G. , Reinikainen, T. , Drakenberg, T.
Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei.
Protein Sci., 6:294 - 303, 1997.(PubMed : 9041630)
Experimental methodSOLUTION NMR
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P62694 ) , eF-site , KEGG ( EC 3.2.1.91 ) , PISA , NRG-CING