Aluminium in PDB 3n5k: Structure of the (Sr)CA2+-Atpase E2-ALF4- Form

All present enzymatic activity of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form:
3.6.3.8;

The structure of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form, PDB code: 3n5k was solved by M.Bublitz, C.Olesen, H.Poulsen, J.P.Morth, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	72.00 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	101.930, 109.420, 276.092, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 21.6

The structure of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Magnesium	(Mg)	2 atoms
Potassium	(K)	2 atoms

The binding sites of Aluminium atom in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form (pdb code 3n5k). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form, PDB code: 3n5k:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Al2002 b:24.9 occ:1.00 AL A:ALF2002 0.0 24.9 1.0 F3 A:ALF2002 1.8 23.1 1.0 F1 A:ALF2002 1.8 27.4 1.0 F4 A:ALF2002 1.8 25.1 1.0 F2 A:ALF2002 1.8 23.4 1.0 OD1 A:ASP351 1.9 23.8 1.0 O A:HOH1365 2.0 23.3 1.0 CG A:ASP351 3.1 24.2 1.0 MG A:MG2001 3.5 26.7 1.0 O A:HOH1279 3.5 23.0 1.0 OD2 A:ASP351 3.6 23.9 1.0 NZ A:LYS684 3.8 22.9 1.0 OG1 A:THR625 3.8 19.3 1.0 O A:THR181 3.9 22.4 1.0 N A:GLY626 3.9 24.8 1.0 N A:THR353 4.0 21.7 1.0 CA A:GLY182 4.1 23.2 1.0 N A:LYS352 4.1 22.6 1.0 OE2 A:GLU183 4.2 22.2 1.0 ND2 A:ASN706 4.2 20.9 1.0 CB A:ASP351 4.3 21.3 1.0 CA A:THR625 4.3 25.9 1.0 CB A:THR353 4.3 19.1 1.0 CB A:THR625 4.5 22.2 1.0 C A:GLY182 4.6 27.3 1.0 C A:THR625 4.6 25.7 1.0 O A:HOH1366 4.6 21.1 1.0 OG1 A:THR353 4.7 21.5 1.0 C A:THR181 4.7 23.8 1.0 CA A:THR353 4.7 21.3 1.0 CA A:ASP351 4.7 21.4 1.0 O A:GLY182 4.7 25.8 1.0 O A:THR353 4.7 23.7 1.0 O A:ILE624 4.8 24.8 1.0 CA A:GLY626 4.8 21.3 1.0 N A:GLY182 4.8 21.9 1.0 C A:LYS352 4.8 23.4 1.0 C A:ASP351 4.8 24.0 1.0 CA A:LYS352 4.9 22.3 1.0 OD1 A:ASP707 4.9 26.2 1.0 CE A:LYS684 5.0 26.1 1.0

Aluminium binding site 2 out of 2 in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Al2002 b:24.9 occ:1.00 AL B:ALF2002 0.0 24.9 1.0 F1 B:ALF2002 1.8 28.6 1.0 F3 B:ALF2002 1.8 23.6 1.0 F4 B:ALF2002 1.8 25.2 1.0 F2 B:ALF2002 1.8 23.3 1.0 O B:HOH1311 1.9 22.3 1.0 OD1 B:ASP351 1.9 22.7 1.0 CG B:ASP351 3.0 26.1 1.0 MG B:MG2001 3.5 28.4 1.0 OD2 B:ASP351 3.5 25.4 1.0 O B:HOH1228 3.5 29.4 1.0 NZ B:LYS684 3.7 23.0 1.0 OG1 B:THR625 3.8 22.5 1.0 O B:THR181 3.9 24.9 1.0 N B:THR353 3.9 26.4 1.0 N B:GLY626 4.0 22.4 1.0 N B:LYS352 4.1 22.2 1.0 OE2 B:GLU183 4.2 24.6 1.0 ND2 B:ASN706 4.2 20.1 1.0 CA B:GLY182 4.2 25.6 1.0 CB B:ASP351 4.3 23.1 1.0 CA B:THR625 4.3 22.1 1.0 CB B:THR353 4.3 23.9 1.0 CB B:THR625 4.5 23.1 1.0 OG1 B:THR353 4.6 25.4 1.0 CA B:THR353 4.7 22.4 1.0 CA B:ASP351 4.7 23.4 1.0 O B:THR353 4.7 25.9 1.0 O B:HOH1226 4.7 27.0 1.0 C B:GLY182 4.7 24.2 1.0 O B:GLY182 4.7 22.6 1.0 C B:THR181 4.7 23.3 1.0 C B:THR625 4.7 22.2 1.0 O B:ILE624 4.8 27.2 1.0 C B:LYS352 4.8 25.7 1.0 CA B:LYS352 4.8 24.2 1.0 C B:ASP351 4.8 24.0 1.0 N B:GLY182 4.9 22.5 1.0 CE B:LYS684 4.9 26.1 1.0 OD1 B:ASP707 4.9 24.5 1.0 CA B:GLY626 4.9 23.4 1.0 OD2 B:ASP707 4.9 26.6 1.0

M.Bublitz, M.Musgaard, H.Poulsen, L.Thogersen, C.Olesen, B.Schiott, J.P.Morth, J.V.Moller, P.Nissen. Ion Pathways in the Sarcoplasmic Reticulum CA2+-Atpase. J.Biol.Chem. V. 288 10759 2013.
ISSN: ISSN 0021-9258
PubMed: 23400778
DOI: 10.1074/JBC.R112.436550