1p5d Summary


Enzyme-ligand complex of P. aeruginosa PMM/PGM

The structure was published by Regni, C., Naught, L., Tipton, P.A., and Beamer, L.J., in 2004 in a paper entitled "Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 2003.

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

The PDB entry contains the structure of Phosphomannomutase. This molecule has the UniProt identifier P26276 (ALGC_PSEAE)search. The sample contained 463 residues which is 100% of the natural sequence. Out of 463 residues 449 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
X Phosphomannomutase P26276 (1-463) (ALGC_PSEAE)search Pseudomonas aeruginosa PAO1search 98% 463 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P26276 (1 - 463) Phosphomannomutase Pseudomonas aeruginosa

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
X (P26276) Phosphoglucomutase, first 3 domainssearch, Phosphoglucomutase, C-terminal domainsearch Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3search, Major birch pollen allergen Bet v 1search PF00408: Phosphoglucomutase/phosphomannomutase, C-terminal domainsearch, PF02878: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain Isearch, PF02879: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain IIsearch, PF02880: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain IIIsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
X (P26276) intramolecular transferase activity, phosphotransferasessearch magnesium ion bindingsearch phosphoglucomutase activitysearch phosphomannomutase activitysearch catalytic activitysearch isomerase activitysearch metal ion bindingsearch carbohydrate metabolic processsearch pathogenesissearch lipopolysaccharide biosynthetic processsearch alginic acid biosynthetic processsearch metabolic processsearch lipopolysaccharide core region biosynthetic processsearch GDP-mannose biosynthetic processsearch O antigen biosynthetic processsearch cytosolsearch

Chain InterPro annotation
X Alpha-D-phosphohexomutase superfamilysearch Alpha-D-phosphohexomutase, C-terminalsearch Alpha-D-phosphohexomutase, alpha/beta/alpha domain Isearch Alpha-D-phosphohexomutase, alpha/beta/alpha domain IIsearch Alpha-D-phosphohexomutase, alpha/beta/alpha domain IIIsearch Alpha-D-phosphohexomutase, alpha/beta/alpha I/II/IIIsearch Alpha-D-phosphohexomutase, conserved sitesearch