Calcium in PDB 1b8l: Calcium-Bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin

The structure of Calcium-Bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin, PDB code: 1b8l was solved by M.S.Cates, M.B.Berry, E.Ho, Q.Li, J.D.Potter, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.511, 37.298, 37.067, 90.00, 113.12, 90.00
R / Rfree (%)	16.8 / 22.7

The binding sites of Calcium atom in the Calcium-Bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin (pdb code 1b8l). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Calcium-Bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin, PDB code: 1b8l:

Calcium binding site 1 out of 1 in the Calcium-Bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Calcium-Bound D51A/E101D/F102W Triple Mutant of Beta Carp Parvalbumin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca110 b:15.4 occ:1.00 OD1 A:ASP94 2.2 16.1 1.0 OD1 A:ASP92 2.2 18.0 1.0 OD2 A:ASP101 2.3 17.3 1.0 O A:LYS96 2.3 15.4 1.0 OD1 A:ASP90 2.3 16.9 1.0 O A:HOH118 2.4 16.6 1.0 CG A:ASP94 3.2 15.0 1.0 CG A:ASP92 3.3 21.3 1.0 CG A:ASP90 3.4 15.3 1.0 CG A:ASP101 3.4 12.5 1.0 C A:LYS96 3.4 14.7 1.0 OD2 A:ASP94 3.6 14.7 1.0 OD2 A:ASP92 3.8 38.5 1.0 OD1 A:ASP101 3.9 15.1 1.0 N A:LYS96 4.1 14.7 1.0 CA A:ASP90 4.1 14.0 1.0 N A:ASP94 4.1 13.2 1.0 CB A:ASP90 4.2 14.7 1.0 OD2 A:ASP90 4.2 17.3 1.0 CA A:LYS96 4.3 14.0 1.0 N A:ILE97 4.3 12.3 1.0 CB A:ASP94 4.4 18.3 1.0 CA A:ILE97 4.4 12.8 1.0 N A:ASP92 4.4 15.9 1.0 N A:GLY93 4.4 13.2 1.0 C A:ASP90 4.5 15.0 1.0 O A:HOH130 4.5 18.1 1.0 N A:GLY98 4.6 14.4 1.0 CB A:ASP92 4.6 21.0 1.0 CB A:ASP101 4.6 12.4 1.0 N A:SER91 4.7 16.9 1.0 CA A:ASP94 4.7 15.7 1.0 N A:GLY95 4.7 16.7 1.0 CB A:LYS96 4.8 21.7 1.0 O A:HOH250 4.8 41.3 1.0 CA A:ASP92 4.9 22.6 1.0 C A:ASP94 5.0 15.8 1.0 C A:ILE97 5.0 12.8 1.0 C A:ASP92 5.0 23.0 1.0

M.S.Cates, M.B.Berry, E.L.Ho, Q.Li, J.D.Potter, G.N.Phillips Jr.. Metal-Ion Affinity and Specificity in Ef-Hand Proteins: Coordination Geometry and Domain Plasticity in Parvalbumin. Structure Fold.Des. V. 7 1269 1999.
ISSN: ISSN 0969-2126
PubMed: 10545326
DOI: 10.1016/S0969-2126(00)80060-X