3CBH

THREE-DIMENSIONAL STRUCTURE OF CELLOBIOHYDROLASE FROM TRICHODERMA REESEI

Summary for 3CBH

Entry DOI	10.2210/pdb3cbh/pdb
Descriptor	CELLOBIOHYDROLASE II CORE PROTEIN (1 entity in total)
Functional Keywords	hydrolase (o-glycosyl)
Biological source	Hypocrea jecorina
Cellular location	Secreted: P07987
Total number of polymer chains	1
Total formula weight	39055.30
Authors	Jones, T.A.,Rouvinen, J. (deposition date: 1990-08-06, release date: 1991-01-15, Last modification date: 2024-02-21)
Primary citation	Rouvinen, J.,Bergfors, T.,Teeri, T.,Knowles, J.K.,Jones, T.A. Three-dimensional structure of cellobiohydrolase II from Trichoderma reesei. Science, 249:380-386, 1990 Cited by PubMed Abstract: The enzymatic degradation of cellulose is an important process, both ecologically and commercially. The three-dimensional structure of a cellulase, the enzymatic core of CBHII from the fungus Trichoderma reesei reveals an alpha-beta protein with a fold similar to but different from the widely occurring barrel topology first observed in triose phosphate isomerase. The active site of CBHII is located at the carboxyl-terminal end of a parallel beta barrel, in an enclosed tunnel through which the cellulose threads. Two aspartic acid residues, located in the center of the tunnel are the probable catalytic residues. PubMed: 2377893 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation