Sodium in PDB 3ar2: Calcium Pump Crystal Structure with Bound Amppcp and CA2+

All present enzymatic activity of Calcium Pump Crystal Structure with Bound Amppcp and CA2+:
3.6.3.8;

The structure of Calcium Pump Crystal Structure with Bound Amppcp and CA2+, PDB code: 3ar2 was solved by C.Toyoshima, S.Yonekura, J.Tsueda, S.Iwasawa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	161.995, 75.306, 151.541, 90.00, 108.97, 90.00
R / Rfree (%)	24.7 / 27.2

The structure of Calcium Pump Crystal Structure with Bound Amppcp and CA2+ also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Sodium atom in the Calcium Pump Crystal Structure with Bound Amppcp and CA2+ (pdb code 3ar2). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Calcium Pump Crystal Structure with Bound Amppcp and CA2+, PDB code: 3ar2:

Sodium binding site 1 out of 1 in the Calcium Pump Crystal Structure with Bound Amppcp and CA2+


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Calcium Pump Crystal Structure with Bound Amppcp and CA2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1000 b:74.6 occ:1.00 O A:HOH3101 2.3 82.4 1.0 O A:ALA714 2.7 85.6 1.0 O A:LYS712 2.9 85.0 1.0 OE2 A:GLU732 3.2 95.1 1.0 O A:GLU715 3.4 88.0 1.0 OE1 A:GLU732 3.5 94.2 1.0 CD A:GLU732 3.5 92.6 1.0 C A:ALA714 3.9 84.7 1.0 C A:LYS712 3.9 84.2 1.0 C A:GLU715 4.0 87.4 1.0 O A:LEU711 4.2 78.7 1.0 CA A:GLU715 4.4 87.6 1.0 CA A:LYS712 4.5 84.2 1.0 N A:GLU715 4.6 86.2 1.0 CG A:GLU732 4.6 91.6 1.0 O A:LYS713 4.6 84.8 1.0 C A:LYS713 4.7 84.0 1.0 N A:ILE716 4.7 86.5 1.0 N A:ALA714 4.9 82.9 1.0 CA A:ALA714 5.0 83.3 1.0

C.Toyoshima, S.Yonekura, J.Tsueda, S.Iwasawa. Trinitrophenyl Derivatives Bind Differently From Parent Adenine Nucleotides to CA2+-Atpase in the Absence of CA2+ Proc.Natl.Acad.Sci.Usa V. 108 1833 2011.
ISSN: ISSN 0027-8424
PubMed: 21239683
DOI: 10.1073/PNAS.1017659108