1aq0 Summary



The structure was published by Muller, J.J., Thomsen, K.K., and Heinemann, U., in 1998 in a paper entitled "Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1997.

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

This PDB entry contains multiple copies of the structure of 1,3-1,4-BETA-GLUCANASE.

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 most likely forms homodimers.

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 1,3-1,4-BETA-GLUCANASE P12257 (7-312) (GUB2_HORVU)search Hordeum vulgaresearch 100% 306 100%
B 1,3-1,4-BETA-GLUCANASE P12257 (7-312) (GUB2_HORVU)search Hordeum vulgaresearch 100% 306 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P12257 (7 - 312) 1,3-1,4-BETA-GLUCANASE Hordeum vulgare

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P12257) beta-glycanasessearch Glycosidasessearch PF00332: Glycosyl hydrolases family 17search

Chain ID Molecular function (GO) Biological process (GO)
A, B (P12257) hydrolase activity, acting on glycosyl bondssearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch licheninase activitysearch hydrolase activitysearch carbohydrate metabolic processsearch metabolic processsearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 17search Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch