Literature summary for 3.2.1.176 extracted from

Parkkinen, T.; Koivula, A.; Vehmaanperae, J.; Rouvinen, J.
Crystal structures of Melanocarpus albomyces cellobiohydrolase Cel7B in complex with cello-oligomers show high flexibility in the substrate binding (2008), Protein Sci., 17, 1383-1394 .

Search for more literature for 3.2.1.176

Cloned(Commentary)

Cloned (Comment)	Organism
-	Melanocarpus albomyces

Crystallization (Commentary)

Crystallization (Comment)	Organism
free and in complex with cellobiose, cellotriose, and cellotetraose, at 1.6-2.1 A resolution. Four molecules in the asymmetric unit, with characteristic fold of a glycoside hydrolase family 7 cellobiohydrolase. The catalytic residues at the reducing end of the tunnel are conserved, and the mechanism is expected to be retaining. Enzyme shows large variations in the amino acid side chain conformations and in the positions of glycosyl units in the different cellooligomer complexes. In each complex structure, all glycosyl residues are in the chair conformation	Melanocarpus albomyces

Crystallization (Comment)

Organism

free and in complex with cellobiose, cellotriose, and cellotetraose, at 1.6-2.1 A resolution. Four molecules in the asymmetric unit, with characteristic fold of a glycoside hydrolase family 7 cellobiohydrolase. The catalytic residues at the reducing end of the tunnel are conserved, and the mechanism is expected to be retaining. Enzyme shows large variations in the amino acid side chain conformations and in the positions of glycosyl units in the different cellooligomer complexes. In each complex structure, all glycosyl residues are in the chair conformation

Melanocarpus albomyces

Organism

Organism	UniProt	Comment	Textmining
Melanocarpus albomyces	Q8J0K6	-	-

Synonyms

Synonyms	Comment	Organism
Cel7B	-	Melanocarpus albomyces

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)