1AZY

STRUCTURAL AND THEORETICAL STUDIES SUGGEST DOMAIN MOVEMENT PRODUCES AN ACTIVE CONFORMATION OF THYMIDINE PHOSPHORYLASE

Summary for 1AZY

DescriptorTHYMIDINE PHOSPHORYLASE (1 entity in total)
Functional Keywordsglycosyltransferase, thymidine phosphorylase, salvage pathway
Biological sourceEscherichia coli
Total number of polymer chains2
Total molecular weight94481.98
Authors
Pugmire, M.J.,Cook, W.J.,Jasanoff, A.,Walter, M.R.,Ealick, S.E. (deposition date: 1997-11-24, release date: 1999-01-13, Last modification date: 2011-07-13)
Primary citation
Pugmire, M.J.,Cook, W.J.,Jasanoff, A.,Walter, M.R.,Ealick, S.E.
Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase.
J.Mol.Biol., 281:285-299, 1998
PubMed: 9698549 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.1998.1941
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (3 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers112.4%4.6%1.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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