1o98 Summary

pdbe.org/1o98
spacer

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)search. 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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE Q9X519 (1-511) (GPMI_GEOSE)search Geobacillus stearothermophilussearch 100% 511 99%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9X519 (1 - 511) 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE Geobacillus stearothermophilus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q9X519) 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domainsearch, 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, catalytic domainsearch 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domainsearch, Alkaline Phosphatase, subunit Asearch PF01676: Metalloenzyme superfamilysearch, PF06415: BPG-independent PGAM N-terminus (iPGM_N)search

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (Q9X519) glucose catabolic processsearch metabolic processsearch glycolytic processsearch metal ion bindingsearch manganese ion bindingsearch phosphoglycerate mutase activitysearch catalytic activitysearch isomerase activitysearch 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activitysearch cytoplasmsearch

Chain InterPro annotation
A Phosphoglycerate mutase, 2,3-bisphosphoglycerate-independentsearch Metalloenzymesearch BPG-independent PGAM, N-terminalsearch Alkaline phosphatase-like, alpha/beta/alphasearch Alkaline-phosphatase-like, core domainsearch