1o08 Summary


Structure of Pentavalent Phosphorous Intermediate of an Enzyme Catalyzed Phosphoryl transfer Reaction observed on cocrystallization with Glucose 1-phosphate

The structure was published by Lahiri, S.D., Zhang, G., Dunaway-Mariano, D., and Allen, K.N., in 2003 in a paper entitled "The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 2003.

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

The PDB entry contains the structure of beta-phosphoglucomutase. This molecule has the UniProt identifier P71447 (PGMB_LACLA)search. The sample contained 221 residues which is 100% of the natural sequence. Out of 221 residues 220 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 beta-phosphoglucomutase P71447 (1-221) (PGMB_LACLA)search Lactococcus lactis subsp. lactis Il1403search 100% 221 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P71447 (1 - 221) beta-phosphoglucomutase Lactococcus lactis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P71447) beta-Phosphoglucomutase-likesearch Rossmann foldsearch, Putative phosphatase; domain 2search PF00702: haloacid dehalogenase-like hydrolasesearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P71447) carbohydrate metabolic processsearch metabolic processsearch magnesium ion bindingsearch beta-phosphoglucomutase activitysearch hydrolase activitysearch isomerase activitysearch metal ion bindingsearch cytoplasmsearch

Chain InterPro annotation
A HAD hydrolase, subfamily IAsearch Beta-phosphoglucomutasesearch Beta-phosphoglucomutase hydrolasesearch Phosphoglycolate phosphatase, domain 2search HAD-like domainsearch