1uqy Summary



The structure was published by Pell, G., Taylor, E.J., Gloster, T.M., et al., Clark, S., Davies, G.J., and Gilbert, H.J., in 2004 in a paper entitled "The Mechanisms by which Family 10 Glycoside Hydrolases Bind Decorated Substrates" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.72 Å and deposited in 2003.

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

The PDB entry contains the structure of ENDOXYLANASE.

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 ENDOXYLANASE O68541 (11-379) (O68541_9GAMM)search Cellvibrio mixtussearch 97% 378 91%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O68541 (11 - 379) ENDOXYLANASE Cellvibrio mixtus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (O68541) beta-glycanasessearch Glycosidasessearch PF00331: Glycosyl hydrolase family 10search

Chain ID Biological process (GO) Molecular function (GO)
A (O68541) carbohydrate metabolic processsearch metabolic processsearch xylan catabolic processsearch hydrolase activitysearch hydrolase activity, acting on glycosyl bondssearch endo-1,4-beta-xylanase activitysearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch

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