1tml Summary



The structure was published by Spezio, M., Wilson, D.B., and Karplus, P.A., in 1993 in a paper entitled "Crystal structure of the catalytic domain of a thermophilic endocellulase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1993.

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

The PDB entry contains the structure of ENDO-1,4-BETA-D-GLUCANASE. This molecule has the UniProt identifier P26222 (GUN2_THEFU)search. The sample contained 286 residues which is < 90% of the natural sequence. Out of 286 residues 286 were observed and are deposited in the PDB.

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 ENDO-1,4-BETA-D-GLUCANASE P26222 (32-317) (GUN2_THEFU)search Thermobifida fuscasearch < 90% 286 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P26222 (32 - 317) ENDO-1,4-BETA-D-GLUCANASE Thermobifida fusca

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

Chain ID Molecular function (GO) Biological process (GO)
A (P26222) hydrolase activity, hydrolyzing O-glycosyl compoundssearch cellulose catabolic processsearch carbohydrate metabolic processsearch

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