1YCP

THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16

Summary for 1YCP

DescriptorEPSILON THROMBIN, ALPHA THROMBIN, FIBRINOPEPTIDE A-ALPHA, ... (6 entities in total)
Functional Keywordsfibrinopeptide-a, complex (serine protease-peptide), thrombin, hydrolase-hydrolase substrate complex, hydrolase/hydrolase substrate
Biological sourceBos taurus (cattle)
Cellular locationSecreted, extracellular space P00735 P00735 P00735 P00735
Secreted P02671
Total number of polymer chains7
Total molecular weight75732.31
Authors
Malkowski, M.G.,Edwards, B.F.P. (deposition date: 1997-05-01, release date: 1998-05-06, Last modification date: 2011-07-13)
Primary citation
Malkowski, M.G.,Martin, P.D.,Lord, S.T.,Edwards, B.F.
Crystal structure of fibrinogen-Aalpha peptide 1-23 (F8Y) bound to bovine thrombin explains why the mutation of Phe-8 to tyrosine strongly inhibits normal cleavage at Arg-16.
Biochem.J., 326:815-822, 1997
PubMed: 9307032 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.5 Å)
?

Structure validation

ClashscoreRamachandran outliersSidechain outliers301.6%13.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report