Aluminium in PDB 1t5t: Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form

All present enzymatic activity of Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form:
3.6.3.8;

The structure of Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form, PDB code: 1t5t was solved by T.L.-M.Sorensen, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	162.477, 75.617, 151.651, 90.00, 108.82, 90.00
R / Rfree (%)	24.6 / 29.3

The structure of Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form also contains other interesting chemical elements:

Fluorine	(F)	4 atoms
Magnesium	(Mg)	2 atoms
Potassium	(K)	1 atom
Calcium	(Ca)	2 atoms

The binding sites of Aluminium atom in the Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form (pdb code 1t5t). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Structure of the (Sr)CA2+-Atpase CA2-E1-Adp:ALF4- Form, PDB code: 1t5t:

Aluminium binding site 1 out of 1 in the Structure of the (Sr)CA2+-Atpase CA2-E1-Adp: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 CA2-E1-Adp:ALF4- Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Al1002 b:44.1 occ:1.00 AL A:ALF1002 0.0 44.1 1.0 F4 A:ALF1002 1.8 39.6 1.0 F2 A:ALF1002 1.8 41.8 1.0 F1 A:ALF1002 1.8 40.0 1.0 F3 A:ALF1002 1.8 39.2 1.0 O3B A:ADP1001 2.0 45.8 1.0 OD1 A:ASP351 2.1 47.7 1.0 CG A:ASP351 3.1 47.1 1.0 PB A:ADP1001 3.2 47.8 1.0 OD2 A:ASP351 3.3 41.9 1.0 MG A:MG1005 3.4 39.7 1.0 O3A A:ADP1001 3.5 44.7 1.0 NZ A:LYS684 3.6 36.8 1.0 O A:HOH1047 3.7 37.1 1.0 OG1 A:THR353 3.7 47.5 1.0 OG1 A:THR625 3.7 47.5 1.0 MG A:MG1007 3.8 66.8 1.0 O2B A:ADP1001 3.8 47.4 1.0 N A:THR353 3.8 47.8 1.0 O A:HOH1008 4.0 60.8 1.0 CB A:THR353 4.0 47.6 1.0 ND2 A:ASN706 4.1 48.4 1.0 N A:GLY626 4.2 45.5 1.0 N A:LYS352 4.2 48.4 1.0 CA A:THR625 4.3 45.9 1.0 CB A:THR625 4.4 45.8 1.0 O A:THR353 4.4 47.5 1.0 CB A:ASP351 4.4 48.0 1.0 CA A:THR353 4.5 47.8 1.0 O1B A:ADP1001 4.5 45.4 1.0 O A:HOH1049 4.6 42.7 1.0 PA A:ADP1001 4.7 46.7 1.0 O1A A:ADP1001 4.7 42.1 1.0 C A:THR625 4.8 45.4 1.0 C A:LYS352 4.8 48.0 1.0 OD1 A:ASN706 4.8 48.5 1.0 O A:ILE624 4.8 46.5 1.0 CE A:LYS684 4.9 39.5 1.0 CA A:ASP351 4.9 48.5 1.0 CA A:LYS352 4.9 48.5 1.0 CG A:ASN706 4.9 46.7 1.0 C A:THR353 5.0 47.9 1.0

T.L.Sorensen, J.V.Moller, P.Nissen. Phosphoryl Transfer and Calcium Ion Occlusion in the Calcium Pump. Science V. 304 1672 2004.
ISSN: ISSN 0036-8075
PubMed: 15192230
DOI: 10.1126/SCIENCE.1099366