1cz1 Summary

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EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS AT 1.85 A RESOLUTION

The structure was published by Cutfield, S.M., Davies, G.J., Murshudov, G., et al., Moody, P.C., Sullivan, P.A., and Cutfield, J.F., in 1999 in a paper entitled "The structure of the exo-beta-(1,3)-glucanase from Candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 1999.

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

The PDB entry contains the structure of PROTEIN (EXO-B-(1,3)-GLUCANASE). This molecule has the UniProt identifier P29717 (EXG1_CANAL)search. The sample contained 394 residues which is 94% of the natural sequence. Out of 394 residues 394 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 PROTEIN (EXO-B-(1,3)-GLUCANASE) P29717 (45-438) (EXG1_CANAL)search Candida albicans SC5314search 94% 394 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P29717 (45 - 438) PROTEIN (EXO-B-(1,3)-GLUCANASE) Candida albicans

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P29717) beta-glycanasessearch Glycosidasessearch PF00150: Cellulase (glycosyl hydrolase family 5)search

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P29717) hydrolase activity, hydrolyzing O-glycosyl compoundssearch hydrolase activitysearch glucan exo-1,3-beta-glucosidase activitysearch transferase activitysearch hydrolase activity, acting on glycosyl bondssearch cell adhesion molecule bindingsearch carbohydrate metabolic processsearch cellular glucan metabolic processsearch metabolic processsearch pathogenesissearch cell adhesionsearch fungal-type cell wall organizationsearch single-species biofilm formation on inanimate substratesearch single-species biofilm formation in or on host organismsearch cell wall organizationsearch cell-substrate adhesionsearch cell surfacesearch extracellular regionsearch cell wallsearch

Chain InterPro annotation
A Glycoside hydrolase, family 5search Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 5, conserved sitesearch