1.4A CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM BACILLUS STEAROTHERMOPHILUS COMPLEXED WITH 2-PHOSPHOGLYCERATE
The structure was published by Rigden, D.J., Mello, L.V., Lamani, E., Littlejohn, J.E., and Jedrzejas, M.J., in 2003 in a paper entitled "Insights Into the Catalytic Mechanism of Cofactor-Independent Phosphoglycerate Mutase from X-Ray Crystallography, Simulated Dynamics and Molecular Modeling" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.4 Å and deposited in 2002.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE. This molecule has the UniProt identifier Q9X519 (GPMI_GEOSE). The sample contained 511 residues which is 100% of the natural sequence. Out of 511 residues 509 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: