1F13
RECOMBINANT HUMAN CELLULAR COAGULATION FACTOR XIII
Summary for 1F13
Entry DOI | 10.2210/pdb1f13/pdb |
Descriptor | CELLULAR COAGULATION FACTOR XIII ZYMOGEN (2 entities in total) |
Functional Keywords | coagulation, transglutaminase, transferase, acyltransferase, blood coagulation, coagulation factor |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm: P00488 |
Total number of polymer chains | 2 |
Total formula weight | 166467.84 |
Authors | Weiss, M.S.,Hilgenfeld, R. (deposition date: 1998-01-16, release date: 1998-08-12, Last modification date: 2024-05-22) |
Primary citation | Weiss, M.S.,Metzner, H.J.,Hilgenfeld, R. Two non-proline cis peptide bonds may be important for factor XIII function. FEBS Lett., 423:291-296, 1998 Cited by PubMed Abstract: The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic crystal form and refined to an R-factor of 18.3% (Rfree = 23.6%) for all data between 40.0 and 2.1 A resolution. Two non-proline cis peptide bonds were detected. One is between Arg310 and Tyr311 close to the active site cysteine residue (Cys314) and the other is between Gln425 and Phe426 at the dimerization interface. The structure and the role of these cis peptides are discussed in the light of their possible importance for factor XIII function. PubMed: 9515726DOI: 10.1016/S0014-5793(98)00098-2 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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