Fluorine in PDB 1xp5: 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: 1xp5 was solved by C.Olesen, T.L.S.Sorensen, R.C.Nielsen, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	80.00 / 3.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	86.510, 119.270, 142.260, 90.00, 90.00, 90.00
R / Rfree (%)	23.7 / 26.5

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

Magnesium	(Mg)	1 atom
Aluminium	(Al)	1 atom
Potassium	(K)	1 atom

The binding sites of Fluorine atom in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form (pdb code 1xp5). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form, PDB code: 1xp5:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F 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:F2002 b:63.0 occ:1.00 F1 A:ALF2002 0.0 63.0 1.0 AL A:ALF2002 1.8 57.1 1.0 F4 A:ALF2002 2.4 58.0 1.0 O A:HOH2005 2.6 51.2 1.0 F3 A:ALF2002 2.6 56.4 1.0 ND2 A:ASN706 2.8 44.2 1.0 O A:HOH2006 2.8 73.4 1.0 OD1 A:ASP351 2.8 47.1 1.0 CA A:GLY182 3.1 28.6 1.0 OD1 A:ASN706 3.2 41.1 1.0 NZ A:LYS684 3.3 32.0 1.0 O A:THR181 3.3 37.7 1.0 CG A:ASN706 3.4 45.9 1.0 MG A:MG2001 3.5 33.4 1.0 F2 A:ALF2002 3.5 42.0 1.0 CG A:ASP351 3.6 41.2 1.0 N A:GLY182 3.6 34.5 1.0 OD2 A:ASP351 3.6 48.5 1.0 C A:THR181 3.7 32.9 1.0 C A:GLY182 4.0 26.6 1.0 O A:GLY182 4.1 28.8 1.0 OE2 A:GLU183 4.2 64.0 1.0 OD2 A:ASP707 4.2 49.1 1.0 OD1 A:ASP707 4.3 50.1 1.0 O A:HOH2004 4.5 64.4 1.0 CG A:ASP707 4.6 52.1 1.0 CE A:LYS684 4.6 43.6 1.0 N A:GLY626 4.6 40.3 1.0 CB A:ASN706 4.9 45.9 1.0 CA A:THR181 4.9 31.5 1.0 CB A:ASP351 4.9 30.8 1.0

Fluorine binding site 2 out of 4 in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F 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 A:F2002 b:42.0 occ:1.00 F2 A:ALF2002 0.0 42.0 1.0 AL A:ALF2002 1.8 57.1 1.0 F3 A:ALF2002 2.5 56.4 1.0 F4 A:ALF2002 2.5 58.0 1.0 OD1 A:ASP351 2.6 47.1 1.0 N A:LYS352 2.7 31.1 1.0 O A:HOH2006 2.7 73.4 1.0 OG1 A:THR625 2.8 47.8 1.0 N A:THR353 2.9 32.3 1.0 CG A:ASP351 3.2 41.2 1.0 CA A:LYS352 3.2 30.5 1.0 CB A:LYS352 3.3 24.6 1.0 CB A:THR625 3.3 41.2 1.0 C A:LYS352 3.4 36.2 1.0 F1 A:ALF2002 3.5 63.0 1.0 OD2 A:ASP351 3.5 48.5 1.0 OE2 A:GLU183 3.8 64.0 1.0 C A:ASP351 3.8 33.1 1.0 CA A:THR625 3.8 38.7 1.0 CB A:THR353 3.9 33.1 1.0 CA A:THR353 3.9 32.5 1.0 OG1 A:THR353 4.0 48.3 1.0 CA A:ASP351 4.1 30.7 1.0 O A:THR353 4.2 33.6 1.0 CB A:ASP351 4.2 30.8 1.0 N A:GLY626 4.3 40.3 1.0 O A:ILE624 4.3 30.3 1.0 MG A:MG2001 4.5 33.4 1.0 C A:THR353 4.5 39.1 1.0 CG A:LYS352 4.5 24.9 1.0 O A:LYS352 4.5 32.1 1.0 C A:THR625 4.6 43.3 1.0 NZ A:LYS684 4.7 32.0 1.0 CG2 A:THR625 4.7 37.4 1.0 O A:ASP351 4.8 40.9 1.0 N A:THR625 4.8 31.9 1.0 CE A:LYS352 4.9 44.7 1.0 O A:HOH2005 4.9 51.2 1.0 CD A:GLU183 5.0 68.8 1.0 C A:ILE624 5.0 35.1 1.0

Fluorine binding site 3 out of 4 in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form within 5.0Å range: probe atom residue distance (Å) B Occ A:F2002 b:56.4 occ:1.00 F3 A:ALF2002 0.0 56.4 1.0 AL A:ALF2002 1.8 57.1 1.0 MG A:MG2001 2.3 33.4 1.0 F2 A:ALF2002 2.5 42.0 1.0 F1 A:ALF2002 2.6 63.0 1.0 O A:THR353 2.7 33.6 1.0 OD2 A:ASP351 2.7 48.5 1.0 O A:HOH2006 3.0 73.4 1.0 CB A:THR353 3.0 33.1 1.0 OD1 A:ASP351 3.0 47.1 1.0 O A:HOH2004 3.2 64.4 1.0 CG A:ASP351 3.2 41.2 1.0 O A:HOH2005 3.3 51.2 1.0 N A:THR353 3.3 32.3 1.0 OE2 A:GLU183 3.4 64.0 1.0 CA A:THR353 3.4 32.5 1.0 C A:THR353 3.4 39.1 1.0 O A:GLY182 3.4 28.8 1.0 F4 A:ALF2002 3.5 58.0 1.0 OG1 A:THR353 3.9 48.3 1.0 CG2 A:THR353 3.9 28.7 1.0 CA A:GLY182 4.0 28.6 1.0 C A:GLY182 4.0 26.6 1.0 C A:LYS352 4.2 36.2 1.0 N A:LYS352 4.3 31.1 1.0 CD A:GLU183 4.4 68.8 1.0 OD2 A:ASP703 4.4 42.4 1.0 O A:THR181 4.5 37.7 1.0 CB A:ASP351 4.7 30.8 1.0 N A:GLY354 4.7 30.0 1.0 OG1 A:THR625 4.8 47.8 1.0 CA A:LYS352 4.8 30.5 1.0 OE1 A:GLU183 4.9 43.3 1.0 O A:LYS352 4.9 32.1 1.0

Fluorine binding site 4 out of 4 in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of the (Sr)CA2+-Atpase E2-ALF4- Form within 5.0Å range: probe atom residue distance (Å) B Occ A:F2002 b:58.0 occ:1.00 F4 A:ALF2002 0.0 58.0 1.0 AL A:ALF2002 1.8 57.1 1.0 O A:HOH2006 2.4 73.4 1.0 F1 A:ALF2002 2.4 63.0 1.0 F2 A:ALF2002 2.5 42.0 1.0 OD1 A:ASP351 2.6 47.1 1.0 NZ A:LYS684 2.8 32.0 1.0 N A:GLY626 2.8 40.3 1.0 CA A:THR625 3.0 38.7 1.0 OG1 A:THR625 3.3 47.8 1.0 C A:THR625 3.3 43.3 1.0 CE A:LYS684 3.5 43.6 1.0 F3 A:ALF2002 3.5 56.4 1.0 CB A:THR625 3.6 41.2 1.0 O A:ILE624 3.6 30.3 1.0 CG A:ASP351 3.8 41.2 1.0 ND2 A:ASN706 3.8 44.2 1.0 CA A:GLY626 3.9 34.7 1.0 O A:THR181 4.0 37.7 1.0 N A:THR625 4.1 31.9 1.0 C A:ILE624 4.3 35.1 1.0 OE2 A:GLU183 4.4 64.0 1.0 OD2 A:ASP351 4.4 48.5 1.0 O A:THR625 4.5 37.2 1.0 N A:LYS352 4.6 31.1 1.0 O A:HOH2005 4.6 51.2 1.0 OD1 A:ASP707 4.7 50.1 1.0 N A:ASP627 4.7 27.8 1.0 C A:THR181 4.8 32.9 1.0 CB A:ASP351 4.8 30.8 1.0 CA A:ASP351 4.9 30.7 1.0 C A:GLY626 4.9 38.1 1.0 CD A:LYS684 4.9 32.6 1.0 CG A:ASN706 4.9 45.9 1.0

C.Olesen, T.L.S.Sorensen, R.C.Nielsen, J.V.Moller, P.Nissen. Dephosphorylation of the Calcium Pump Coupled to Counterion Occlusion Science V. 306 2251 2004.
ISSN: ISSN 0036-8075
PubMed: 15618517
DOI: 10.1126/SCIENCE.1106289