1AVC
BOVINE ANNEXIN VI (CALCIUM-BOUND)
Summary for 1AVC
Entry DOI | 10.2210/pdb1avc/pdb |
Descriptor | ANNEXIN VI, CALCIUM ION (3 entities in total) |
Functional Keywords | annexin, calcium-binding, membrane-binding, calcium/phospholipid-binding protein, calcium-phospholipid-binding protein complex |
Biological source | Bos taurus (cattle) |
Total number of polymer chains | 1 |
Total formula weight | 76251.97 |
Authors | Avila-Sakar, A.J.,Creutz, C.E.,Kretsinger, R.H. (deposition date: 1997-09-16, release date: 1998-01-28, Last modification date: 2024-05-22) |
Primary citation | Avila-Sakar, A.J.,Creutz, C.E.,Kretsinger, R.H. Crystal structure of bovine annexin VI in a calcium-bound state. Biochim.Biophys.Acta, 1387:103-116, 1998 Cited by PubMed Abstract: The crystal structure of a calcium-bound form of bovine annexin VI has been determined with X-ray diffraction data to 2.9 A by molecular replacement. Six Ca2+ ions were found, five in AB loops, one in a DE loop. Two loops (II-AB, which binds calcium, and V-AB, which does not) have conformations that differ significantly from those in calcium-free, human recombinant annexin VI. There are only small differences between the calci- and the apo-annexin VI in the rest of the molecule. Calcium by itself does not promote a major conformational change. PubMed: 9748523DOI: 10.1016/S0167-4838(98)00111-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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