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Magnesium in PDB 4hqj: Crystal Structure of Na+,K+-Atpase in the Na+-Bound State

Enzymatic activity of Crystal Structure of Na+,K+-Atpase in the Na+-Bound State

All present enzymatic activity of Crystal Structure of Na+,K+-Atpase in the Na+-Bound State:
3.6.3.9;

Protein crystallography data

The structure of Crystal Structure of Na+,K+-Atpase in the Na+-Bound State, PDB code: 4hqj was solved by M.Nyblom, L.Reinhard, P.Gourdon, P.Nissen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 4.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 109.073, 219.578, 261.958, 90.00, 90.00, 90.00
R / Rfree (%) 26.1 / 28.8

Other elements in 4hqj:

The structure of Crystal Structure of Na+,K+-Atpase in the Na+-Bound State also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Aluminium (Al) 2 atoms
Sodium (Na) 6 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Na+,K+-Atpase in the Na+-Bound State (pdb code 4hqj). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Na+,K+-Atpase in the Na+-Bound State, PDB code: 4hqj:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4hqj

Go back to Magnesium Binding Sites List in 4hqj
Magnesium binding site 1 out of 2 in the Crystal Structure of Na+,K+-Atpase in the Na+-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Na+,K+-Atpase in the Na+-Bound State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1103

b:0.5
occ:1.00
F3 A:ALF1102 1.7 0.9 1.0
OD2 A:ASP710 2.1 1.0 1.0
O A:THR371 2.1 0.3 1.0
OD2 A:ASP369 2.1 0.9 1.0
CG A:ASP710 3.1 0.5 1.0
CG A:ASP369 3.2 0.8 1.0
C A:THR371 3.2 0.8 1.0
AL A:ALF1102 3.3 0.3 1.0
F1 A:ALF1102 3.4 0.2 1.0
OD1 A:ASP710 3.5 0.2 1.0
OD1 A:ASP369 3.7 0.8 1.0
CA A:THR371 4.0 0.3 1.0
CB A:THR371 4.0 0.7 1.0
O3B A:ADP1101 4.0 0.4 1.0
F2 A:ALF1102 4.1 0.3 1.0
N A:GLY711 4.1 0.9 1.0
N A:THR371 4.2 0.6 1.0
N A:GLY372 4.2 0.8 1.0
OD2 A:ASP714 4.2 0.6 1.0
OG1 A:THR373 4.3 0.3 1.0
CB A:ASP710 4.4 0.1 1.0
OD1 A:ASP714 4.4 0.3 1.0
CB A:ASP369 4.4 0.1 1.0
CA A:GLY372 4.5 0.7 1.0
CA A:GLY711 4.5 0.6 1.0
O2B A:ADP1101 4.7 0.5 1.0
CG2 A:THR371 4.7 0.7 1.0
CG A:ASP714 4.8 0.8 1.0
N A:ASP710 4.8 0.2 1.0
PB A:ADP1101 4.9 0.6 1.0
C A:LYS370 4.9 0.3 1.0
OD1 A:ASN713 4.9 0.9 1.0
N A:THR373 5.0 0.2 1.0

Magnesium binding site 2 out of 2 in 4hqj

Go back to Magnesium Binding Sites List in 4hqj
Magnesium binding site 2 out of 2 in the Crystal Structure of Na+,K+-Atpase in the Na+-Bound State


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Na+,K+-Atpase in the Na+-Bound State within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg1103

b:0.3
occ:1.00
F3 C:ALF1102 1.7 0.3 1.0
O C:THR371 2.1 0.6 1.0
OD2 C:ASP710 2.1 0.8 1.0
OD2 C:ASP369 2.1 0.1 1.0
CG C:ASP710 3.1 0.8 1.0
CG C:ASP369 3.2 0.4 1.0
C C:THR371 3.2 0.9 1.0
AL C:ALF1102 3.3 0.9 1.0
F1 C:ALF1102 3.4 0.9 1.0
OD1 C:ASP710 3.5 0.9 1.0
O2B C:ADP1101 3.6 0.6 1.0
OD1 C:ASP369 3.6 0.1 1.0
CA C:THR371 3.9 0.5 1.0
CB C:THR371 4.0 0.2 1.0
O3B C:ADP1101 4.1 0.9 1.0
F2 C:ALF1102 4.1 0.2 1.0
N C:THR371 4.1 0.8 1.0
N C:GLY711 4.1 0.5 1.0
N C:GLY372 4.2 0.3 1.0
OD2 C:ASP714 4.2 0.1 1.0
OG1 C:THR373 4.3 0.2 1.0
CB C:ASP710 4.4 0.1 1.0
PB C:ADP1101 4.4 0.8 1.0
CA C:GLY372 4.4 0.9 1.0
CB C:ASP369 4.4 0.2 1.0
OD1 C:ASP714 4.5 0.4 1.0
CA C:GLY711 4.5 0.6 1.0
CG2 C:THR371 4.7 0.9 1.0
CG C:ASP714 4.8 0.1 1.0
N C:ASP710 4.8 0.3 1.0
C C:LYS370 4.9 0.5 1.0
N C:THR373 4.9 0.9 1.0
CA C:ASP710 5.0 0.5 1.0
C C:ASP710 5.0 0.7 1.0
OD1 C:ASN713 5.0 0.7 1.0

Reference:

M.Nyblom, H.Poulsen, P.Gourdon, L.Reinhard, M.Andersson, E.Lindahl, N.Fedosova, P.Nissen. Crystal Structure of Na+, K(+)-Atpase in the Na(+)-Bound State. Science V. 342 123 2013.
ISSN: ISSN 0036-8075
PubMed: 24051246
DOI: 10.1126/SCIENCE.1243352
Page generated: Mon Dec 14 17:56:07 2020

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