1uz4 Summary

pdbe.org/1uz4
spacer

COMMON INHIBITION OF BETA-GLUCOSIDASE AND BETA-MANNOSIDASE BY ISOFAGOMINE LACTAM REFLECTS DIFFERENT CONFORMATIONAL INTINERARIES FOR GLUCOSIDE AND MANNOSIDE HYDROLYSIS

The structure was published by Vincent, F., Gloster, T.M., Macdonald, J., et al., Fontes, C.M.G.A., Gilbert, H.J., and Davies, G.J., in 2004 in a paper entitled "Common Inhibition of Both Beta-Glucosidases and Beta-Mannosidases by Isofagomine Lactam Reflects Different Conformational Itineraries for Pyranoside Hydrolysis" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.71 Å and deposited in 2004.

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

The PDB entry contains the structure of MAN5A.

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 MAN5A Q6QT42 (26-456) (Q6QT42_9GAMM)search Cellvibrio mixtussearch 95% 440 93%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q6QT42 (26 - 456) MAN5A Cellvibrio mixtus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A beta-glycanasessearch Glycosidasessearch Cellulase (glycosyl hydrolase family 5)search

Chain ID Molecular function (GO) Biological process (GO)
A (Q6QT42) hydrolase activity, hydrolyzing O-glycosyl compoundssearch carbohydrate metabolic processsearch

Chain InterPro annotation
A Glycoside hydrolase, family 5search Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch