1exp Summary



The structure was published by White, A., Tull, D., Johns, K., Withers, S.G., and Rose, D.R., in 1996 in a paper entitled "Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1996.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of BETA-1,4-D-GLYCANASE CEX-CD.

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 is most likely monomeric.

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 BETA-1,4-D-GLYCANASE CEX-CD P07986 (42-353) (GUX_CELFI)search Cellulomonas fimisearch < 90% 312 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07986 (42 - 353) BETA-1,4-D-GLYCANASE CEX-CD Cellulomonas fimi

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A beta-glycanasessearch Glycosidasessearch Glycosyl hydrolase family 10search

Chain ID Molecular function (GO) Biological process (GO)
A (P07986) hydrolase activity, hydrolyzing O-glycosyl compoundssearch carbohydrate metabolic processsearch

Chain InterPro annotation
A Glycoside hydrolase, family 10search Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch