Magnesium in PDB 8qmp: Structure of the E2 Beryllium Fluoride Complex of the Autoinhibited Calcium Atpase ACA8

Enzymatic activity of Structure of the E2 Beryllium Fluoride Complex of the Autoinhibited Calcium Atpase ACA8

All present enzymatic activity of Structure of the E2 Beryllium Fluoride Complex of the Autoinhibited Calcium Atpase ACA8:
7.2.2.10;

Other elements in 8qmp:

The structure of Structure of the E2 Beryllium Fluoride Complex of the Autoinhibited Calcium Atpase ACA8 also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the E2 Beryllium Fluoride Complex of the Autoinhibited Calcium Atpase ACA8 (pdb code 8qmp). 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 Structure of the E2 Beryllium Fluoride Complex of the Autoinhibited Calcium Atpase ACA8, PDB code: 8qmp:

Magnesium binding site 1 out of 1 in 8qmp

Go back to Magnesium Binding Sites List in 8qmp
Magnesium binding site 1 out of 1 in the Structure of the E2 Beryllium Fluoride Complex of the Autoinhibited Calcium Atpase ACA8


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the E2 Beryllium Fluoride Complex of the Autoinhibited Calcium Atpase ACA8 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1101

b:43.0
occ:1.00
OD1 A:ASP785 2.0 47.8 1.0
O A:THR484 2.0 33.1 1.0
OD2 A:ASP482 2.0 30.6 1.0
F2 A:BEF1102 2.1 47.5 1.0
CG A:ASP785 2.9 47.6 1.0
CG A:ASP482 3.1 32.5 1.0
OD2 A:ASP785 3.1 50.4 1.0
H A:GLY786 3.1 48.1 1.0
C A:THR484 3.2 32.3 1.0
HB A:THR484 3.2 36.2 1.0
BE A:BEF1102 3.3 39.4 1.0
OD1 A:ASP482 3.8 40.9 1.0
N A:GLY786 3.8 47.7 1.0
HA3 A:GLY485 3.8 38.1 1.0
H A:ASP785 3.8 46.7 1.0
HA3 A:GLY786 3.8 48.9 1.0
H A:THR484 3.8 36.5 1.0
F3 A:BEF1102 3.9 44.8 1.0
HB3 A:ASP482 3.9 32.6 1.0
CA A:THR484 4.0 36.4 1.0
CB A:THR484 4.0 34.3 1.0
O A:SER305 4.1 41.8 1.0
HA2 A:GLY309 4.1 43.0 1.0
CB A:ASP482 4.1 30.2 1.0
N A:THR484 4.1 41.3 1.0
H A:THR486 4.2 35.0 1.0
N A:GLY485 4.2 33.9 1.0
CB A:ASP785 4.3 43.4 1.0
CA A:GLY786 4.3 48.7 1.0
CA A:GLY485 4.4 38.5 1.0
F1 A:BEF1102 4.5 34.2 1.0
OD2 A:ASP789 4.5 42.9 1.0
HB2 A:ASP482 4.5 32.0 1.0
N A:ASP785 4.5 46.1 1.0
HD21 A:ASN788 4.6 42.2 1.0
HB3 A:ASP785 4.6 45.6 1.0
C A:ASP785 4.6 46.0 1.0
HA2 A:GLY786 4.7 48.0 1.0
CA A:ASP785 4.7 40.5 1.0
OD1 A:ASN788 4.8 42.6 1.0
HA A:SER306 4.8 56.2 1.0
H A:LYS483 4.8 29.1 1.0
N A:THR486 4.9 33.8 1.0
OG1 A:THR484 4.9 33.1 1.0
HG22 A:THR484 4.9 38.1 1.0
HB2 A:ASP785 4.9 46.0 1.0
HA A:THR484 4.9 35.9 1.0
CA A:GLY309 5.0 41.7 1.0
HA3 A:GLY309 5.0 42.4 1.0
HB3 A:SER305 5.0 47.0 1.0

Reference:

S.T.Larsen, J.K.Dannerso, C.J.F.Nielsen, L.R.Poulsen, M.Palmgren, P.Nissen. Conserved N-Terminal Regulation of the ACA8 Calcium Pump with Two Calmodulin Binding Sites. J.Mol.Biol. V. 436 68747 2024.
ISSN: ESSN 1089-8638
PubMed: 39168442
DOI: 10.1016/J.JMB.2024.168747
Page generated: Thu Oct 31 21:59:10 2024

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