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Sodium in PDB 3ar9: Calcium Pump Crystal Structure with Bound BEF3, Tnp-Amp and Tg in the Absence of Calcium

Enzymatic activity of Calcium Pump Crystal Structure with Bound BEF3, Tnp-Amp and Tg in the Absence of Calcium

All present enzymatic activity of Calcium Pump Crystal Structure with Bound BEF3, Tnp-Amp and Tg in the Absence of Calcium:
3.6.3.8;

Protein crystallography data

The structure of Calcium Pump Crystal Structure with Bound BEF3, Tnp-Amp and Tg in the Absence of Calcium, PDB code: 3ar9 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) 14.97 / 2.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 90.388, 135.807, 105.425, 90.00, 90.00, 90.00
R / Rfree (%) 21.3 / 25.7

Other elements in 3ar9:

The structure of Calcium Pump Crystal Structure with Bound BEF3, Tnp-Amp and Tg in the Absence of Calcium also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Magnesium (Mg) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Calcium Pump Crystal Structure with Bound BEF3, Tnp-Amp and Tg in the Absence of Calcium (pdb code 3ar9). 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 BEF3, Tnp-Amp and Tg in the Absence of Calcium, PDB code: 3ar9:

Sodium binding site 1 out of 1 in 3ar9

Go back to Sodium Binding Sites List in 3ar9
Sodium binding site 1 out of 1 in the Calcium Pump Crystal Structure with Bound BEF3, Tnp-Amp and Tg in the Absence of Calcium


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 BEF3, Tnp-Amp and Tg in the Absence of Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1000

b:54.5
occ:1.00
 O A:ALA714 2.5 48.4 1.0
OE1 A:GLU732 2.6 65.2 1.0
OE2 A:GLU732 2.7 68.6 1.0
O A:LEU711 2.8 57.8 1.0
O A:LYS712 2.9 54.8 1.0
CD A:GLU732 3.0 65.4 1.0
N A:GLY717 3.4 49.7 1.0
C A:LYS712 3.5 58.0 1.0
C A:ALA714 3.6 48.8 1.0
CA A:LYS712 3.7 58.2 1.0
OE1 A:GLN244 3.7 73.6 1.0
C A:LEU711 3.8 54.1 1.0
CA A:GLY717 3.9 48.6 1.0
O A:GLU715 4.0 54.8 1.0
O A:ALA730 4.0 63.5 1.0
C A:ILE716 4.1 47.7 1.0
C A:GLU715 4.1 50.4 1.0
N A:ALA714 4.2 52.3 1.0
N A:LYS712 4.2 57.3 1.0
N A:ILE716 4.3 50.6 1.0
CA A:ALA714 4.3 49.7 1.0
CA A:ILE716 4.3 48.3 1.0
CG A:GLU732 4.5 64.3 1.0
CB A:ALA714 4.5 47.5 1.0
N A:LYS713 4.6 54.5 1.0
N A:GLU715 4.7 49.6 1.0
C A:LYS713 4.7 53.8 1.0
CA A:GLU715 4.8 51.4 1.0
CD A:GLN244 4.9 73.0 1.0

Reference:

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
Page generated: Mon Oct 7 05:52:01 2024

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