Phosphopentomutase from Bacillus cereus bound to glucose-1,6-bisphosphate

Summary for 3OT9

Related3M8W 3M8Y 3M8Z
DescriptorPhosphopentomutase, MANGANESE (II) ION, GLYCEROL, ... (5 entities in total)
Functional Keywordsalkaline phosphatase like core domain, phosphopentomutase, ribose-5-phosphate, ribose-1-phosphate, glucose-1, 6-bisphosphate, phosphoryl transfer, isomerase
Biological sourceBacillus cereus
Cellular locationCytoplasm (By similarity) Q818Z9
Total number of polymer chains3
Total molecular weight134883.75
Panosian, T.D.,Nannemann, D.P.,Watkins, G.,Phalen, V.,Wadzinski, B.,Bachmann, B.O.,Iverson, T.M. (deposition date: 2010-09-10, release date: 2010-12-29, Last modification date: 2020-07-29)
Primary citation
Panosian, T.D.,Nannemann, D.P.,Watkins, G.R.,Phelan, V.V.,McDonald, W.H.,Wadzinski, B.E.,Bachmann, B.O.,Iverson, T.M.
Bacillus cereus Phosphopentomutase Is an Alkaline Phosphatase Family Member That Exhibits an Altered Entry Point into the Catalytic Cycle.
J.Biol.Chem., 286:8043-8054, 2011
PubMed: 21193409 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M110.201350
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.1923 0.1% 1.8% 2.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-10-14