1PVB
X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMIN
Summary for 1PVB
Entry DOI | 10.2210/pdb1pvb/pdb |
Descriptor | PARVALBUMIN, CALCIUM ION, AMMONIUM ION, ... (4 entities in total) |
Functional Keywords | calcium binding protein |
Biological source | Esox lucius (northern pike) |
Total number of polymer chains | 1 |
Total formula weight | 11528.03 |
Authors | Declercq, J.P.,Tinant, B.,Parello, J. (deposition date: 1995-01-05, release date: 1995-02-27, Last modification date: 2024-10-23) |
Primary citation | Declercq, J.P.,Tinant, B.,Parello, J. X-ray structure of a new crystal form of pike 4.10 beta parvalbumin. Acta Crystallogr.,Sect.D, 52:165-169, 1996 Cited by PubMed Abstract: A new crystal form of pike (pI 4.10) parvalbumin has been crystallized in presence of EDTA at pH 8.0. The crystals are orthorhombic, space group P2(1)2(1)2(1), with a = 51.84, b = 49.95, c = 34.96 A. Diffractometer data were collected to 1.75 A. The structure was solved by molecular replacement and refined to R = 0.168 for 7774 observed reflections [I>/= 2sigma(I)] in the range 8.0-1.75 A. In spite of the presence of EDTA, calcium ions are present in both primary binding sites. As compared to the previously reported structures, the main differences concern the conformation of the N-terminal residues and the packing in the unit cell. PubMed: 15299738DOI: 10.1107/S0907444995010006 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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