3zj7 Summary


Crystal structure of strictosidine glucosidase in complex with inhibitor-1

A publication describing this structure is not available. The depositing authors are Xia, L.search; Lin, H.search; Panjikar, S.search; Ruppert, M.search; Castiglia, A.search; Rajendran, C.search; Wang, M.search; Schuebel, H.search; Warzecha, H.search; Jaeger, V.search; Stoeckigt, J.search

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2013.

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

This PDB entry contains multiple copies of the structure of STRICTOSIDINE-O-BETA-D-GLUCOSIDASE.

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 STRICTOSIDINE-O-BETA-D-GLUCOSIDASE Q8GU20 (1-532) (SG1_RAUSE)search Rauvolfia serpentinasearch 100% 532 87%
B STRICTOSIDINE-O-BETA-D-GLUCOSIDASE Q8GU20 (1-532) (SG1_RAUSE)search Rauvolfia serpentinasearch 100% 532 87%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q8GU20 (1 - 532) STRICTOSIDINE-O-BETA-D-GLUCOSIDASE Rauvolfia serpentina

Chain Sequence family (Pfam)
A, B (Q8GU20) PF00232: Glycosyl hydrolase family 1search

Chain ID Biological process (GO) Molecular function (GO)
A, B (Q8GU20) alkaloid metabolic processsearch alkaloid biosynthetic processsearch metabolic processsearch carbohydrate metabolic processsearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch strictosidine beta-glucosidase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch

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