Magnesium in PDB 1b8c: Parvalbumin

The structure of Parvalbumin, PDB code: 1b8c 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)	40.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	35.231, 50.211, 55.374, 90.00, 99.22, 90.00
R / Rfree (%)	19.7 / 30

The binding sites of Magnesium atom in the Parvalbumin (pdb code 1b8c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Parvalbumin, PDB code: 1b8c:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Parvalbumin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Parvalbumin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg308 b:13.7 occ:1.00 OD1 A:ASP90 1.9 9.8 1.0 OD2 A:ASP101 2.0 8.1 1.0 O A:LYS96 2.0 16.0 1.0 OD1 A:ASP92 2.1 28.6 1.0 OD1 A:ASP94 2.1 12.3 1.0 O A:HOH580 2.3 16.1 1.0 CG A:ASP94 3.0 25.4 1.0 CG A:ASP92 3.1 19.9 1.0 CG A:ASP90 3.1 16.9 1.0 CG A:ASP101 3.1 12.0 1.0 C A:LYS96 3.2 10.3 1.0 OD2 A:ASP94 3.4 23.9 1.0 OD2 A:ASP92 3.4 21.4 1.0 OD1 A:ASP101 3.7 16.0 1.0 CA A:ASP90 3.8 10.2 1.0 CB A:ASP90 3.9 16.4 1.0 N A:LYS96 3.9 10.1 1.0 N A:ASP94 3.9 21.0 1.0 OD2 A:ASP90 4.0 14.2 1.0 N A:ILE97 4.0 11.8 1.0 CA A:ILE97 4.1 12.5 1.0 CA A:LYS96 4.1 9.0 1.0 C A:ASP90 4.2 16.3 1.0 N A:GLY93 4.2 21.4 1.0 N A:ASP92 4.3 19.4 1.0 CB A:ASP94 4.3 21.9 1.0 N A:GLY98 4.3 10.6 1.0 CB A:ASP101 4.3 4.2 1.0 CB A:ASP92 4.4 13.0 1.0 N A:GLY95 4.5 12.7 1.0 CA A:ASP94 4.5 19.1 1.0 O A:HOH415 4.5 3.8 1.0 N A:SER91 4.6 18.4 1.0 C A:ASP92 4.6 21.4 1.0 CA A:ASP92 4.6 16.5 1.0 C A:ILE97 4.7 12.2 1.0 C A:ASP94 4.7 19.1 1.0 O A:ASP90 4.7 17.9 1.0 C A:GLY93 4.8 23.6 1.0 CA A:GLY93 5.0 24.3 1.0

Magnesium binding site 2 out of 2 in the Parvalbumin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Parvalbumin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg309 b:6.1 occ:1.00 OD1 B:ASP289 1.9 7.4 1.0 O B:LYS295 1.9 6.8 1.0 O B:HOH664 2.0 30.5 1.0 OD2 B:ASP300 2.0 9.7 1.0 OD1 B:ASP291 2.2 6.1 1.0 OD1 B:ASP293 2.2 14.6 1.0 C B:LYS295 3.1 6.2 1.0 CG B:ASP289 3.1 2.6 1.0 CG B:ASP300 3.1 17.5 1.0 CG B:ASP291 3.2 1.5 1.0 CG B:ASP293 3.2 12.0 1.0 OD2 B:ASP291 3.5 6.2 1.0 OD1 B:ASP300 3.6 18.5 1.0 OD2 B:ASP293 3.7 8.1 1.0 N B:LYS295 3.8 14.4 1.0 N B:ASP293 3.8 10.0 1.0 CB B:ASP289 3.9 6.7 1.0 N B:ILE296 3.9 3.3 1.0 CA B:ASP289 3.9 8.2 1.0 CA B:ILE296 4.0 9.3 1.0 OD2 B:ASP289 4.0 5.7 1.0 CA B:LYS295 4.0 12.2 1.0 O B:HOH421 4.1 6.3 1.0 N B:GLY297 4.2 2.7 1.0 N B:GLY292 4.3 13.6 1.0 CB B:ASP293 4.3 16.1 1.0 CB B:ASP300 4.4 12.4 1.0 C B:ASP289 4.4 2.2 1.0 N B:ASP291 4.4 19.7 1.0 CA B:ASP293 4.5 16.3 1.0 CB B:ASP291 4.5 9.6 1.0 N B:GLY294 4.5 13.2 1.0 C B:ILE296 4.6 9.3 1.0 CG B:LYS295 4.6 21.3 1.0 C B:ASP291 4.7 15.9 1.0 C B:ASP293 4.7 20.2 1.0 CA B:ASP291 4.7 14.0 1.0 N B:SER290 4.8 13.6 1.0 C B:GLY292 4.8 10.9 1.0 CA B:GLY292 4.8 9.8 1.0 O B:ASP289 4.9 6.8 1.0 CB B:LYS295 4.9 21.3 1.0 C B:GLY294 5.0 9.7 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