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Aluminium in PDB 1xp5: Structure of the (Sr)CA2+-Atpase E2-ALF4- Form

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1xp5:

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

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

Aluminium Binding Sites:

The binding sites of Aluminium 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 Aluminium atom.
In total only one binding site of Aluminium was determined in the Structure of the (Sr)CA2+-Atpase E2-ALF4- Form, PDB code: 1xp5:

Aluminium binding site 1 out of 1 in 1xp5

Go back to Aluminium Binding Sites List in 1xp5
Aluminium binding site 1 out of 1 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:57.1
occ:1.00
AL A:ALF2002 0.0 57.1 1.0
F2 A:ALF2002 1.8 42.0 1.0
F1 A:ALF2002 1.8 63.0 1.0
F3 A:ALF2002 1.8 56.4 1.0
F4 A:ALF2002 1.8 58.0 1.0
O A:HOH2006 2.1 73.4 1.0
OD1 A:ASP351 2.1 47.1 1.0
CG A:ASP351 3.0 41.2 1.0
OD2 A:ASP351 3.2 48.5 1.0
OE2 A:GLU183 3.5 64.0 1.0
O A:HOH2005 3.5 51.2 1.0
MG A:MG2001 3.6 33.4 1.0
NZ A:LYS684 3.7 32.0 1.0
OG1 A:THR625 3.7 47.8 1.0
O A:THR181 3.9 37.7 1.0
N A:LYS352 4.0 31.1 1.0
N A:GLY626 4.1 40.3 1.0
N A:THR353 4.1 32.3 1.0
O A:THR353 4.3 33.6 1.0
CA A:GLY182 4.3 28.6 1.0
CB A:THR353 4.3 33.1 1.0
ND2 A:ASN706 4.3 44.2 1.0
CB A:ASP351 4.3 30.8 1.0
CA A:THR625 4.3 38.7 1.0
CB A:THR625 4.4 41.2 1.0
O A:GLY182 4.4 28.8 1.0
C A:GLY182 4.6 26.6 1.0
CA A:THR353 4.7 32.5 1.0
CA A:ASP351 4.7 30.7 1.0
OG1 A:THR353 4.7 48.3 1.0
CD A:GLU183 4.7 68.8 1.0
O A:HOH2004 4.7 64.4 1.0
C A:THR181 4.7 32.9 1.0
O A:ILE624 4.8 30.3 1.0
C A:THR625 4.8 43.3 1.0
C A:LYS352 4.8 36.2 1.0
CE A:LYS684 4.8 43.6 1.0
C A:ASP351 4.8 33.1 1.0
CA A:LYS352 4.8 30.5 1.0
OD1 A:ASP707 4.9 50.1 1.0
OD1 A:ASN706 4.9 41.1 1.0
C A:THR353 4.9 39.1 1.0
N A:GLY182 4.9 34.5 1.0

Reference:

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
Page generated: Sat Dec 12 01:30:47 2020

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