1pvb

X-RAY STRUCTURE OF A NEW CRYSTAL FORM OF PIKE 4.10 PARVALBUMIN

spinqualitylabelsall models 1pvb, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pvb is a 1 chain structure with sequence from Esox lucius. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: ACE, CA, NH4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PRVB_ESOLU In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. X-ray structure of a new crystal form of pike 4.10 beta parvalbumin.,Declercq JP, Tinant B, Parello J Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):165-9. PMID:15299738 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Parvalbumin

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