1bg4 Summary



The structure was published by Schmidt, A., Schlacher, A., Steiner, W., Schwab, H., and Kratky, C., in 1998 in a paper entitled "Structure of the xylanase from Penicillium simplicissimum." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.75 Å and deposited in 1998.

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

The PDB entry contains the structure of ENDO-1,4-BETA-XYLANASE. This molecule has the UniProt identifier P56588 (XYNA_PENSI)search. The sample contained 302 residues which is 100% of the natural sequence. Out of 302 residues 302 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-XYLANASE P56588 (2-302) (XYNA_PENSI)search Penicillium simplicissimumsearch 100% 302 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P56588 (2 - 302) ENDO-1,4-BETA-XYLANASE Penicillium simplicissimum

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P56588) beta-glycanasessearch Glycosidasessearch PF00331: Glycosyl hydrolase family 10search

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P56588) carbohydrate metabolic processsearch xylan catabolic processsearch polysaccharide catabolic processsearch metabolic processsearch hydrolase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch endo-1,4-beta-xylanase activitysearch extracellular regionsearch

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