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Sodium in PDB 3nam: Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg

Enzymatic activity of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg

All present enzymatic activity of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg:
3.6.3.8;

Protein crystallography data

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg, PDB code: 3nam was solved by A.M.L.Winther, Y.Sonntag, C.Olesen, J.V.Moller, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 3.10
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 71.545, 71.545, 591.227, 90.00, 90.00, 90.00
R / Rfree (%) 23.9 / 28

Other elements in 3nam:

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg (pdb code 3nam). 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 Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg, PDB code: 3nam:

Sodium binding site 1 out of 1 in 3nam

Go back to Sodium Binding Sites List in 3nam
Sodium binding site 1 out of 1 in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dotg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na995

b:46.0
occ:1.00
 OE2 A:GLU732 2.6 87.5 1.0
O A:ALA714 2.7 80.4 1.0
O A:LYS712 2.8 73.1 1.0
O A:LEU711 2.8 77.7 1.0
OE1 A:GLU732 3.3 90.5 1.0
CD A:GLU732 3.3 87.6 1.0
C A:LYS712 3.4 74.7 1.0
NE2 A:GLN244 3.4 0.7 1.0
O A:HOH999 3.4 79.2 1.0
CA A:LYS712 3.5 74.2 1.0
C A:LEU711 3.8 74.8 1.0
O A:GLU715 3.9 79.4 1.0
C A:ALA714 3.9 80.3 1.0
N A:LYS712 4.2 74.0 1.0
N A:GLY717 4.2 76.4 1.0
C A:GLU715 4.2 79.6 1.0
O A:ALA730 4.3 76.7 1.0
CD A:GLN244 4.3 0.3 1.0
N A:LYS713 4.4 76.0 1.0
N A:ALA714 4.5 80.8 1.0
OE1 A:GLN244 4.5 0.8 1.0
N A:ILE716 4.6 79.7 1.0
C A:LYS713 4.7 80.1 1.0
CB A:LYS712 4.8 74.0 1.0
CA A:ILE716 4.8 77.3 1.0
CG A:GLU732 4.8 84.7 1.0
CA A:GLU715 4.8 80.6 1.0
CA A:ALA714 4.8 80.3 1.0
N A:GLU715 4.8 80.7 1.0
CG A:LYS712 4.9 77.2 1.0
C A:ILE716 4.9 76.3 1.0
CA A:GLY717 4.9 76.8 1.0

Reference:

A.M.L.Winther, H.Liu, Y.Sonntag, C.Olesen, M.Le Maire, H.Soehoel, C.E.Olsen, S.B.Christensen, P.Nissen, J.V.Moller. Critical Roles of Hydrophobicity and Orientation of Side Chains For Inactivation of Sarcoplasmic Reticulum CA2+-Atpase with Thapsigargin and Thapsigargin Analogs J.Biol.Chem. V. 285 28883 2010.
ISSN: ISSN 0021-9258
PubMed: 20551329
DOI: 10.1074/JBC.M110.136242
Page generated: Mon Oct 7 11:47:30 2024

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