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). 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):
This entry contains 1 unique UniProt protein: