1qk2 Summary



The structure was published by Zou, J.-Y., Kleywegt, G.J., Stahlberg, J., et al., Koivula, A., Teeri, T.T., and Jones, T.A., in 1999 in a paper entitled "Crystallographic Evidence for Substrate Ring Distortion and Protein Conformational Changes During Catalysis in Cellobiohydrolase Cel6A from Trichoderma Reesei" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1999.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of CELLOBIOHYDROLASE CEL6A (FORMERLY CALLED CBH II).

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CELLOBIOHYDROLASE CEL6A (FORMERLY CALLED CBH II) P07987 (109-471) (GUX2_HYPJE)search Trichoderma reeseisearch < 90% 363 100%
B CELLOBIOHYDROLASE CEL6A (FORMERLY CALLED CBH II) P07987 (109-471) (GUX2_HYPJE)search Trichoderma reeseisearch < 90% 363 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07987 (109 - 471) CELLOBIOHYDROLASE CEL6A (FORMERLY CALLED CBH II) Trichoderma reesei

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Glycosyl hydrolases family 6, cellulasessearch 7-stranded glycosidases (cellulases)search Glycosyl hydrolases family 6search

Chain ID Biological process (GO) Molecular function (GO)
A, B (P07987) cellulose catabolic processsearch carbohydrate metabolic processsearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 6, conserved sitesearch 1, 4-beta cellobiohydrolasesearch