2w5f Summary


High resolution crystallographic structure of the Clostridium thermocellum N-terminal endo-1,4-beta-D-xylanase 10B (Xyn10B) CBM22-1- GH10 modules complexed with xylohexaose

The structure was published by Najmudin, S., Pinheiro, B.A., Prates, J.A.M., Gilbert, H.J., Romao, M.J., and Fontes, C.M.G.A., in 2010 in a paper entitled "Putting an N-Terminal End to the Clostridium Thermocellum Xylanase Xyn10B Story: Crystal Structure of the Cbm22-1-Gh10 Modules Complexed with Xylohexaose." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2008.

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

This PDB entry contains multiple copies of the structure of ENDO-1,4-BETA-XYLANASE Y.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 Y Not available
Ruminiclostridium thermocellumsearch < 90% 540 95%
B ENDO-1,4-BETA-XYLANASE Y P51584 (32-551) (XYNY_CLOTM)search Ruminiclostridium thermocellumsearch < 90% 540 95%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P51584 (32 - 551) ENDO-1,4-BETA-XYLANASE Y Ruminiclostridium thermocellum

Chain Structural classification (CATH) Sequence family (Pfam)
A, B Galactose-binding domain-likesearch, Glycosidasessearch Glycosyl hydrolase family 10search, Carbohydrate binding domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A, B (P51584) carbohydrate metabolic processsearch hydrolase activity, acting on glycosyl bondssearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 10search Carbohydrate-binding, CenC-likesearch Galactose-binding domain-likesearch Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch