1CI7

TERNARY COMPLEX OF THYMIDYLATE SYNTHASE FROM PNEUMOCYSTIS CARINII

Summary for 1CI7

DescriptorPROTEIN (THYMIDYLATE SYNTHASE), 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, ... (4 entities in total)
Functional Keywordsmethyltransferase, nucleotide biosynthesis, half-sites reactivity, transferase
Biological sourcePneumocystis carinii
Total number of polymer chains2
Total molecular weight69900.4
Authors
Anderson, A.C.,O'Neil, R.H.,Delano, W.L.,Stroud, R.M. (deposition date: 1999-04-08, release date: 2000-04-10, Last modification date: 2011-07-13)
Primary citation
Anderson, A.C.,O'Neil, R.H.,DeLano, W.L.,Stroud, R.M.
The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits.
Biochemistry, 38:13829-13836, 1999
PubMed: 10529228 (PDB entries with the same primary citation)
DOI: 10.1021/bi991610i
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.6 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers505.0%8.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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