2pbg Summary



The structure was published by Wiesmann, C., Hengstenberg, W., and Schulz, G.E., in 1997 in a paper entitled "Crystal structures and mechanism of 6-phospho-beta-galactosidase from Lactococcus lactis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1997.

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

The PDB entry contains the structure of 6-PHOSPHO-BETA-D-GALACTOSIDASE. This molecule has the UniProt identifier P11546 (LACG_LACLL)search. The sample contained 468 residues which is 100% of the natural sequence. Out of 468 residues 468 were observed and are deposited in the PDB.

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 6-PHOSPHO-BETA-D-GALACTOSIDASE P11546 (1-468) (LACG_LACLL)search Lactococcus lactis subsp. lactissearch 100% 468 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P11546 (1 - 468) 6-PHOSPHO-BETA-D-GALACTOSIDASE Lactococcus lactis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P11546) Family 1 of glycosyl hydrolasesearch Glycosidasessearch PF00232: Glycosyl hydrolase family 1search

Chain ID Molecular function (GO) Biological process (GO)
A (P11546) hydrolase activity, hydrolyzing O-glycosyl compoundssearch 6-phospho-beta-galactosidase activitysearch hydrolase activity, acting on glycosyl bondssearch hydrolase activitysearch carbohydrate metabolic processsearch lactose catabolic processsearch metabolic processsearch lactose catabolic process via tagatose-6-phosphatesearch

Chain InterPro annotation
A Glycoside hydrolase, family 1search 6-phospho-beta-galactosidasesearch Glycoside hydrolase, catalytic domainsearch Glycoside hydrolase superfamilysearch Glycoside hydrolase, family 1, active sitesearch