1DM4

SER195ALA MUTANT OF HUMAN THROMBIN COMPLEXED WITH FIBRINOPEPTIDE A (7-16)

Summary for 1DM4

• Entry DOI: 10.2210/pdb1dm4/pdb
• Descriptor: PROTEIN (ALPHA THROMBIN:LIGHT CHAIN), PROTEIN (MUTANT ALPHA THROMBIN:HEAVY CHAIN), PROTEIN (FIBRINOPEPTIDE), ... (4 entities in total)
• Functional Keywords: mutant thrombin, residual catalytic activity, fibrinopeptide a, hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted, extracellular space: P00734 P00734
• Total number of polymer chains: 3
• Total formula weight: 34907.90

Authors

Krishnan, R.,Sadler, E.J.,Tulinsky, A. (deposition date: 1999-12-13, release date: 2000-01-19, Last modification date: 2024-10-16)

Primary citation

Krishnan, R.,Sadler, J.E.,Tulinsky, A.
Structure of the Ser195Ala mutant of human alpha--thrombin complexed with fibrinopeptide A(7--16): evidence for residual catalytic activity.
Acta Crystallogr.,Sect.D, 56:406-410, 2000

PubMed Abstract: The Ser195Ala mutant of human alpha-thrombin was complexed with fibrinopeptide A(7-22) (FPA) in an effort to describe the (P1'-P6') post-cleavage binding subsites of the fibrinogen-recognition exosite and define more clearly the nature of the Michaelis complex and the scissile peptide bond bound at the catalytic site. The thrombin mutant, however, has residual catalytic activity and proteolysis occurred at the Arg16-Gly17 bond. Thus, the structure of the thrombin complex determined was that of FPA(7-16) bound at the active site, which is very similar to the ternary FPA(7-16)cmk-human thrombin-hirugen complex (r.m.s.d. approximately 0.4 A; Stubbs et al. , 1992). It is further shown by subsidiary experiments that the cleavage is the result of residual catalytic activity of the altered catalytic machinery.

PubMed: 10739913
DOI: 10.1107/S0907444900001487

Experimental method

X-RAY DIFFRACTION (2.5 Å)