2cet Summary

pdbe.org/2cet
spacer

BETA-GLUCOSIDASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH PHENETHYL-SUBSTITUTED GLUCOIMIDAZOLE

The structure was published by Gloster, T.M., Roberts, S., Perugino, G., et al., Terinek, M., Vasella, A., and Davies, G.J., in 2006 in a paper entitled "Structural, Kinetic, and Thermodynamic Analysis of Glucoimidazole-Derived Glycosidase Inhibitors." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.97 Å and deposited in 2006.

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

This PDB entry contains multiple copies of the structure of BETA-GLUCOSIDASE A.

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 BETA-GLUCOSIDASE A Q08638 (2-446) (BGLA_THEMA)search Thermotoga maritima MSB8search 100% 468 94%
B BETA-GLUCOSIDASE A Q08638 (2-446) (BGLA_THEMA)search Thermotoga maritima MSB8search 100% 468 94%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q08638 (2 - 446) BETA-GLUCOSIDASE A Thermotoga maritima

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q08638) Family 1 of glycosyl hydrolasesearch Glycosidasessearch PF00232: Glycosyl hydrolase family 1search

Chain ID Biological process (GO) Molecular function (GO)
A, B (Q08638) cellulose catabolic processsearch metabolic processsearch carbohydrate metabolic processsearch polysaccharide catabolic processsearch beta-glucosidase activitysearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch

Chain InterPro annotation
A, B Glycoside hydrolase, family 1search Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase, family 1, beta-glucosidasesearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 1, active sitesearch