1AKE

STRUCTURE OF THE COMPLEX BETWEEN ADENYLATE KINASE FROM ESCHERICHIA COLI AND THE INHIBITOR AP5A REFINED AT 1.9 ANGSTROMS RESOLUTION: A MODEL FOR A CATALYTIC TRANSITION STATE

Summary for 1AKE

DescriptorADENYLATE KINASE, BIS(ADENOSINE)-5'-PENTAPHOSPHATE (3 entities in total)
Functional Keywordstransferase(phosphotransferase)
Biological sourceEscherichia coli
Cellular locationCytoplasm P69441
Total number of polymer chains2
Total molecular weight49072.79
Authors
Mueller, C.W.,Schulz, G.E. (deposition date: 1991-11-08, release date: 1994-01-31, Last modification date: 2011-07-13)
Primary citation
Muller, C.W.,Schulz, G.E.
Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state.
J.Mol.Biol., 224:159-177, 1992
PubMed: 1548697 (PDB entries with the same primary citation)
DOI: 10.1016/0022-2836(92)90582-5
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers50.2%3.4%0.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution