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

Entry DOI	10.2210/pdb1ycp/pdb
Descriptor	EPSILON THROMBIN, ALPHA THROMBIN, FIBRINOPEPTIDE A-ALPHA, ... (6 entities in total)
Functional Keywords	fibrinopeptide-a, complex (serine protease-peptide), thrombin, hydrolase-hydrolase substrate complex, hydrolase/hydrolase substrate
Biological source	Bos taurus (cattle) More
Cellular location	Secreted, extracellular space: P00735 P00735 P00735 P00735 Secreted: P02671
Total number of polymer chains	7
Total formula weight	75732.31
Authors	Malkowski, M.G.,Edwards, B.F.P. (deposition date: 1997-05-01, release date: 1998-05-06, Last modification date: 2021-11-03)
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 Cited by PubMed: 9307032 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation