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: 2024-10-09) |
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: 9307032PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
Download full validation report