2exo Summary

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CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE BETA-1,4-GLYCANASE CEX FROM CELLULOMONAS FIMI

The structure was published by White, A., Withers, S.G., Gilkes, N.R., and Rose, D.R., in 1994 in a paper entitled "Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from Cellulomonas fimi." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1994.

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

The PDB entry contains the structure of EXO-1,4-BETA-D-GLYCANASE. This molecule has the UniProt identifier P07986 (GUX_CELFI)search. The sample contained 312 residues which is < 90% of the natural sequence. Out of 312 residues 312 were observed and are deposited in the PDB.

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 EXO-1,4-BETA-D-GLYCANASE 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) EXO-1,4-BETA-D-GLYCANASE Cellulomonas fimi

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

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

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