Aluminium in PDB 3b9r: Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin

All present enzymatic activity of Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin:
3.6.3.8;

The structure of Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin, PDB code: 3b9r was solved by C.Olesen, M.Picard, A.M.L.Winther, 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)	19.99 / 3.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	131.980, 94.430, 136.180, 90.00, 107.79, 90.00
R / Rfree (%)	18.5 / 23.5

The structure of Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin 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 Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin (pdb code 3b9r). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin, PDB code: 3b9r:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in the Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin within 5.0Å range: probe atom residue distance (Å) B Occ A:Al995 b:50.2 occ:1.00 AL A:ALF995 0.0 50.2 1.0 F4 A:ALF995 1.8 47.6 1.0 F1 A:ALF995 1.8 49.3 1.0 F2 A:ALF995 1.8 18.5 1.0 F3 A:ALF995 1.8 48.1 1.0 O A:HOH1001 1.9 58.6 1.0 OD1 A:ASP351 2.0 54.5 1.0 CG A:ASP351 3.2 49.5 1.0 O A:HOH999 3.4 41.4 1.0 MG A:MG996 3.6 23.8 1.0 NZ A:LYS684 3.7 41.3 1.0 OG1 A:THR625 3.7 33.5 1.0 N A:THR353 3.8 52.9 1.0 OD2 A:ASP351 3.8 55.4 1.0 N A:LYS352 3.9 34.8 1.0 N A:GLY626 4.0 45.1 1.0 OE2 A:GLU183 4.1 59.0 1.0 CA A:THR625 4.2 45.2 1.0 CB A:ASP351 4.3 42.4 1.0 O A:THR181 4.3 42.2 1.0 CB A:THR353 4.3 41.8 1.0 O A:THR353 4.4 50.5 1.0 CA A:GLY182 4.4 25.7 1.0 ND2 A:ASN706 4.4 47.4 1.0 O A:GLY182 4.5 51.2 1.0 CB A:THR625 4.5 41.7 1.0 CA A:ASP351 4.6 45.9 1.0 CA A:THR353 4.6 38.0 1.0 C A:THR625 4.6 46.6 1.0 C A:GLY182 4.7 50.2 1.0 C A:ASP351 4.7 50.3 1.0 CA A:LYS352 4.7 41.7 1.0 C A:LYS352 4.7 49.5 1.0 O A:ILE624 4.8 47.6 1.0 OG1 A:THR353 4.8 58.9 1.0 CB A:LYS352 4.9 28.4 1.0 CA A:GLY626 5.0 41.7 1.0 C A:THR353 5.0 48.9 1.0

Aluminium binding site 2 out of 2 in the Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Serca CA2+-Atpase E2 Aluminium Fluoride Complex Without Thapsigargin within 5.0Å range: probe atom residue distance (Å) B Occ B:Al995 b:69.7 occ:1.00 AL B:ALF995 0.0 69.7 1.0 F2 B:ALF995 1.8 50.6 1.0 F3 B:ALF995 1.8 42.6 1.0 F4 B:ALF995 1.8 61.1 1.0 F1 B:ALF995 1.8 60.2 1.0 O B:HOH1001 1.8 39.8 1.0 OD1 B:ASP351 1.9 69.0 1.0 CG B:ASP351 3.0 66.5 1.0 NZ B:LYS684 3.5 56.4 1.0 O B:HOH1000 3.6 49.1 1.0 OD2 B:ASP351 3.6 56.2 1.0 MG B:MG996 3.7 43.1 1.0 OG1 B:THR625 3.8 56.2 1.0 O B:THR181 3.9 54.8 1.0 CA B:GLY182 4.0 58.5 1.0 OE2 B:GLU183 4.0 72.9 1.0 N B:LYS352 4.0 59.7 1.0 N B:GLY626 4.0 59.3 1.0 N B:THR353 4.2 70.3 1.0 CB B:ASP351 4.2 69.6 1.0 CA B:THR625 4.3 72.7 1.0 CB B:THR353 4.5 53.1 1.0 C B:GLY182 4.5 55.1 1.0 O B:GLY182 4.5 56.8 1.0 OG1 B:THR353 4.6 68.1 1.0 O B:THR353 4.6 57.8 1.0 CA B:ASP351 4.6 78.0 1.0 C B:ASP351 4.6 77.1 1.0 CE B:LYS684 4.6 61.2 1.0 CB B:THR625 4.7 62.2 1.0 O B:ILE624 4.7 84.1 1.0 C B:THR181 4.7 55.5 1.0 C B:THR625 4.7 76.8 1.0 ND2 B:ASN706 4.7 54.7 1.0 CA B:LYS352 4.8 65.2 1.0 N B:GLY182 4.8 53.6 1.0 C B:LYS352 4.8 70.4 1.0 CA B:THR353 4.9 52.9 1.0 CB B:LYS352 4.9 73.2 1.0 OD1 B:ASN706 5.0 45.7 1.0 OD1 B:ASP707 5.0 67.0 1.0 CA B:GLY626 5.0 56.2 1.0

C.Olesen, M.Picard, A.M.L.Winther, C.Gyrup, J.P.Morth, C.Oxvig, J.V.Moller, P.Nissen. The Structural Basis of Calcium Transport By the Calcium Pump Nature V. 450 1036 2007.
ISSN: ISSN 0028-0836
PubMed: 18075584
DOI: 10.1038/NATURE06418