Magnesium in PDB 4pal: Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments

The structure of Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments, PDB code: 4pal was solved by J.P.Declercq, B.Tinant, J.Parello, J.Rambaud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.500, 57.500, 87.400, 90.00, 90.00, 90.00
R / Rfree (%)	18 / n/a

The structure of Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Magnesium atom in the Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments (pdb code 4pal). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments, PDB code: 4pal:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg110 b:12.5 occ:1.00 OE1 A:GLU101 2.0 12.7 1.0 OD2 A:ASP90 2.1 16.3 1.0 OD1 A:ASP92 2.1 11.2 1.0 O A:MET96 2.1 18.6 1.0 O A:HOH246 2.1 15.6 1.0 OD1 A:ASP94 2.2 15.5 1.0 CD A:GLU101 3.1 25.7 1.0 CG A:ASP94 3.1 19.4 1.0 CG A:ASP90 3.1 17.4 1.0 CG A:ASP92 3.2 23.9 1.0 C A:MET96 3.3 24.8 1.0 OE2 A:GLU101 3.4 16.6 1.0 OD2 A:ASP94 3.4 19.6 1.0 OD2 A:ASP92 3.5 17.6 1.0 N A:ASP94 3.9 23.9 1.0 CB A:ASP90 3.9 13.9 1.0 OD1 A:ASP90 3.9 14.7 1.0 CA A:ASP90 4.0 19.5 1.0 N A:MET96 4.0 15.4 1.0 O A:HOH238 4.1 42.6 1.0 CA A:ILE97 4.2 19.1 1.0 N A:GLY98 4.2 10.8 1.0 N A:ILE97 4.2 16.5 1.0 CB A:ASP94 4.3 20.0 1.0 CA A:MET96 4.3 15.7 1.0 N A:ASP92 4.3 15.7 1.0 N A:GLY93 4.3 16.0 1.0 CG A:GLU101 4.4 12.9 1.0 C A:ASP90 4.4 17.8 1.0 CA A:ASP94 4.5 20.8 1.0 CB A:ASP92 4.5 18.3 1.0 C A:ASP92 4.6 17.4 1.0 CG A:MET96 4.6 17.2 1.0 N A:GLY95 4.6 18.5 1.0 CA A:ASP92 4.6 13.6 1.0 C A:ILE97 4.6 19.7 1.0 N A:LYS91 4.8 11.4 1.0 C A:ASP94 4.8 27.9 1.0 O A:ASP90 4.9 20.4 1.0 C A:GLY93 4.9 27.2 1.0

Magnesium binding site 2 out of 2 in the Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg223 b:22.5 occ:1.00 O A:HOH256 2.1 16.2 1.0 O A:HOH231 2.1 19.1 1.0 O A:HOH257 2.2 16.8 1.0 OD2 A:ASP53 2.2 15.8 1.0 O A:HOH230 2.2 20.4 1.0 O A:HOH287 2.3 26.6 1.0 CG A:ASP53 3.0 19.8 1.0 CB A:ASP53 3.5 10.8 1.0 OE1 A:GLU62 3.9 18.3 1.0 OD1 A:ASP53 4.0 21.1 1.0 OD2 A:ASP61 4.1 26.3 1.0 O A:HOH267 4.3 34.2 1.0 OE1 A:GLU59 4.3 15.4 1.0 OD1 A:ASP61 4.4 23.9 1.0 CD A:GLU62 4.5 13.6 1.0 CG A:ASP61 4.7 28.1 1.0 CG A:GLU62 4.7 15.0 1.0 CA A:ASP53 4.8 10.1 1.0 N A:ASP53 4.9 10.4 1.0 CA A:CA111 5.0 14.7 1.0

J.P.Declercq, B.Tinant, J.Parello, J.Rambaud. Ionic Interactions with Parvalbumins. Crystal Structure Determination of Pike 4.10 Parvalbumin in Four Different Ionic Environments. J.Mol.Biol. V. 220 1017 1991.
ISSN: ISSN 0022-2836
PubMed: 1880797
DOI: 10.1016/0022-2836(91)90369-H