Calcium in PDB 1b8r: Parvalbumin

The structure of Parvalbumin, PDB code: 1b8r was solved by M.S.Cates, M.B.Berry, E.L.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)	15.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	28.850, 60.590, 54.480, 90.00, 94.97, 90.00
R / Rfree (%)	17.7 / 27

The binding sites of Calcium atom in the Parvalbumin (pdb code 1b8r). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Parvalbumin, PDB code: 1b8r:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Parvalbumin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Parvalbumin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca109 b:18.6 occ:1.00 O A:LYS96 2.4 13.1 1.0 OD1 A:ASP90 2.4 16.8 1.0 OD1 A:ASP94 2.4 17.8 1.0 OE1 A:GLU101 2.5 17.2 1.0 O A:HOH131 2.5 19.4 0.7 OD1 A:ASP92 2.5 22.8 1.0 OE2 A:GLU101 2.6 21.3 1.0 CD A:GLU101 2.9 16.4 1.0 CG A:ASP90 3.4 14.2 1.0 CG A:ASP94 3.4 22.3 1.0 CG A:ASP92 3.4 24.8 1.0 C A:LYS96 3.6 15.2 1.0 OD2 A:ASP92 3.8 26.1 1.0 OD2 A:ASP94 3.9 21.9 1.0 CA A:ASP90 4.1 16.4 1.0 CB A:ASP90 4.1 8.1 1.0 OD2 A:ASP90 4.2 21.1 1.0 N A:ASP94 4.2 19.5 1.0 N A:LYS96 4.3 17.0 1.0 N A:ASP92 4.4 23.1 1.0 CA A:ILE97 4.4 11.4 1.0 N A:ILE97 4.4 10.3 1.0 CG A:GLU101 4.4 17.2 1.0 O A:HOH166 4.4 27.5 0.6 C A:ASP90 4.5 22.6 1.0 CA A:LYS96 4.5 16.7 1.0 CB A:ASP94 4.5 23.1 1.0 N A:GLY93 4.6 20.7 1.0 N A:GLY98 4.6 12.3 1.0 CB A:ASP92 4.7 22.3 1.0 N A:SER91 4.7 21.4 1.0 CA A:ASP92 4.8 20.0 1.0 CA A:ASP94 4.8 21.1 1.0 N A:GLY95 4.9 18.3 1.0 C A:ASP92 4.9 21.9 1.0 CG A:LYS96 5.0 19.5 1.0

Calcium binding site 2 out of 2 in the Parvalbumin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Parvalbumin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca110 b:13.0 occ:1.00 OD1 A:ASP51 2.3 9.2 1.0 O A:PHE57 2.4 13.4 1.0 OD1 A:ASP53 2.5 18.6 1.0 OE1 A:GLU59 2.5 19.2 1.0 OE1 A:GLU62 2.5 9.3 1.0 OG A:SER55 2.6 14.1 1.0 OE2 A:GLU62 2.7 11.7 1.0 CD A:GLU62 2.9 10.2 1.0 CD A:GLU59 3.3 24.5 1.0 CG A:ASP51 3.5 13.3 1.0 CG A:ASP53 3.5 13.3 1.0 OE2 A:GLU59 3.5 19.1 1.0 C A:PHE57 3.6 8.5 1.0 CB A:SER55 3.8 9.5 1.0 N A:SER55 4.0 11.7 1.0 OD2 A:ASP53 4.0 16.0 1.0 CA A:ASP51 4.1 11.7 1.0 N A:ASP53 4.2 11.5 1.0 OD2 A:ASP51 4.3 11.9 1.0 N A:GLU59 4.3 10.9 1.0 N A:PHE57 4.3 9.1 1.0 CB A:ASP51 4.3 8.5 1.0 O A:HOH161 4.3 32.2 0.6 O A:HOH126 4.3 12.5 0.8 C A:ASP51 4.3 11.8 1.0 CA A:ILE58 4.4 6.0 1.0 CA A:SER55 4.4 9.7 1.0 N A:ILE58 4.4 10.9 1.0 CG A:GLU62 4.5 10.3 1.0 CA A:PHE57 4.5 6.4 1.0 N A:LYS54 4.5 14.4 1.0 N A:GLN52 4.6 9.6 1.0 CB A:ASP53 4.6 11.9 1.0 CA A:ASP53 4.7 12.7 1.0 CG A:GLU59 4.7 17.9 1.0 C A:ASP53 4.8 15.4 1.0 O A:ASP51 4.8 13.6 1.0 N A:GLY56 4.8 8.2 1.0 C A:ILE58 4.9 10.9 1.0 C A:SER55 5.0 9.5 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