1bqc Summary



The structure was published by Hilge, M., Gloor, S.M., Rypniewski, W., et al., Zimmermann, W., Winterhalter, K., and Piontek, K., in 1998 in a paper entitled "High-resolution native and complex structures of thermostable beta-mannanase from Thermomonospora fusca - substrate specificity in glycosyl hydrolase family 5." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 1998.

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

The PDB entry contains the structure of PROTEIN (BETA-MANNANASE). This molecule has the UniProt identifier Q9ZF13 (Q9ZF13_THEFU)search. The sample contained 302 residues which is 100% of the natural sequence. Out of 302 residues 301 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 (BETA-MANNANASE) Q9ZF13 (1-279) (Q9ZF13_THEFU)search Thermobifida fuscasearch 100% 302 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9ZF13 (1 - 279) PROTEIN (BETA-MANNANASE) Thermobifida fusca

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q9ZF13) beta-glycanasessearch Glycosidasessearch PF00150: Cellulase (glycosyl hydrolase family 5)search

Chain ID Molecular function (GO) Biological process (GO)
A (Q9ZF13) mannan endo-1,4-beta-mannosidase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch metabolic processsearch

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