1tux Summary

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HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE XYLANASE FROM THERMOASCUS AURANTIACUS

The structure was published by Natesh, R., Bhanumoorthy, P., Vithayathil, P.J., Sekar, K., Ramakumar, S., and Viswamitra, M.A., in 1999 in a paper entitled "Crystal structure at 1.8 A resolution and proposed amino acid sequence of a thermostable xylanase from Thermoascus aurantiacus." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1998.

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

The PDB entry contains the structure of XYLANASE. This molecule has the UniProt identifier P23360 (XYNA_THEAU)search. The sample contained 301 residues which is 98% of the natural sequence. Out of 301 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 XYLANASE P23360 (28-325) (XYNA_THEAU)search Thermoascus aurantiacussearch 98% 301 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P23360 (28 - 325) XYLANASE Thermoascus aurantiacus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P23360) beta-glycanasessearch Glycosidasessearch PF00331: Glycosyl hydrolase family 10search

Chain ID Molecular function (GO) Biological process (GO)
A (P23360) hydrolase activity, acting on glycosyl bondssearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch endo-1,4-beta-xylanase activitysearch hydrolase activitysearch carbohydrate metabolic processsearch xylan catabolic processsearch polysaccharide catabolic processsearch metabolic processsearch

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