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Potassium in PDB 3nal: Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dtb

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

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

Protein crystallography data

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dtb, PDB code: 3nal 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) 50.00 / 2.65
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 71.330, 71.330, 591.020, 90.00, 90.00, 90.00
R / Rfree (%) 25.5 / 28.3

Other elements in 3nal:

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

Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dtb (pdb code 3nal). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dtb, PDB code: 3nal:

Potassium binding site 1 out of 1 in 3nal

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Sr Ca(2+)-Atpase in the HNE2 State Complexed with the Thapsigargin Derivative Dtb within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K995

b:67.2
occ:1.00
O A:ALA714 2.8 59.0 1.0
OE1 A:GLU732 2.9 52.0 1.0
NE2 A:GLN244 3.0 98.5 1.0
O A:LEU711 3.2 54.9 1.0
O A:HOH1057 3.2 59.8 1.0
O A:LYS712 3.3 54.8 1.0
OE2 A:GLU732 3.3 58.2 1.0
CD A:GLU732 3.4 57.7 1.0
C A:LYS712 3.6 55.9 1.0
O A:HOH1058 3.6 61.7 1.0
C A:ALA714 3.8 59.3 1.0
CA A:LYS712 3.8 57.1 1.0
N A:GLY717 3.9 51.5 1.0
O A:GLU715 4.0 52.6 1.0
C A:GLU715 4.1 53.7 1.0
CD A:GLN244 4.2 97.3 1.0
N A:ALA714 4.2 60.7 1.0
C A:LEU711 4.2 52.2 1.0
N A:LYS713 4.3 56.7 1.0
N A:ILE716 4.3 51.3 1.0
C A:ILE716 4.5 50.1 1.0
N A:LYS712 4.5 55.6 1.0
CA A:ILE716 4.5 49.5 1.0
CA A:ALA714 4.5 59.0 1.0
C A:LYS713 4.5 60.8 1.0
CA A:GLY717 4.6 50.6 1.0
N A:GLU715 4.6 58.6 1.0
O A:ALA730 4.6 55.5 1.0
CA A:GLU715 4.6 56.2 1.0
CG A:GLU732 4.7 55.7 1.0
CG A:GLN244 4.8 94.2 1.0
CA A:LYS713 4.9 59.5 1.0
CB A:ALA714 4.9 60.1 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: Sun Dec 13 23:20:36 2020

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