4BDV
CRYSTAL STRUCTURE OF A TRUNCATED B-DOMAIN HUMAN FACTOR VIII
Summary for 4BDV
Entry DOI | 10.2210/pdb4bdv/pdb |
Related | 1CFG 1D7P 1IQD |
Descriptor | FACTOR VIIIA HEAVY CHAIN, 92 KDA ISOFORM, B DOMAIN, FACTOR VIIIA LIGHT CHAIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
Functional Keywords | blood clotting, blood coagulation, metal binding |
Biological source | HOMO SAPIENS (HUMAN) More |
Total number of polymer chains | 2 |
Total formula weight | 167977.58 |
Authors | Svensson, L.A.,Thim, L.,Olsen, O.H.,Nicolaisen, E.M. (deposition date: 2012-10-08, release date: 2013-05-15, Last modification date: 2024-10-23) |
Primary citation | Svensson, L.A.,Thim, L.,Olsen, O.H.,Nicolaisen, E.M. Evaluation of the Metal Binding Sites in a Recombinant Coagulation Factor Viii Identifies Two Sites with Unique Metal Binding Properties. Biol.Chem., 394:761-, 2013 Cited by PubMed Abstract: Coagulation factor VIII is a glycosylated, non-covalent heterodimer consisting of a heavy chain (A1-A2-B domains) and a light chain (A3-C1-C2 domains). The association of the chains, and the stability and function of the dimer depend on the presence of metal ions. We applied X-ray fluorescence, X-ray crystallographic structure determination with anomalous signals at different wavelengths, and colorimetric measurements to evaluate the metal binding sites in a recombinant factor VIII molecule, turoctocog alfa. We identified a metal binding site in domain A3 dominated by Cu(+) binding and a site in domain A1 dominated by Zn(2+) binding. PubMed: 23435097DOI: 10.1515/HSZ-2012-0298 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.98 Å) |
Structure validation
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