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Magnesium in PDB 3nan: Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg

Enzymatic activity of Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg

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

Protein crystallography data

The structure of Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg, PDB code: 3nan 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) 45.00 / 3.10
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 71.330, 71.330, 589.210, 90.00, 90.00, 90.00
R / Rfree (%) 24.2 / 27.7

Other elements in 3nan:

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

Potassium (K) 1 atom

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 3nan

Go back to Magnesium Binding Sites List in 3nan
Magnesium binding site 1 out of 1 in the Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Sr Ca(2+)-Atpase in the HNE2 State Complexed with A Thapsigargin Derivative Boc-(Phi)Tg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg996

b:75.3
occ:1.00
 OD1 A:ASP703 2.5 81.3 1.0
OD2 A:ASP703 3.2 80.9 1.0
CG A:ASP703 3.2 78.6 1.0
OD2 A:ASP707 3.5 65.4 1.0
OD1 A:ASP707 4.1 68.9 1.0
CG A:ASP707 4.2 65.7 1.0
ND2 A:ASN706 4.4 76.9 1.0
OD2 A:ASP351 4.5 77.3 1.0
N A:ASP703 4.6 72.1 1.0
CB A:ASP703 4.7 74.4 1.0
NZ A:LYS684 4.7 60.6 1.0
N A:GLY704 4.8 71.5 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 Dec 14 08:28:07 2020

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