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Magnesium in PDB 2zbf: Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium

Enzymatic activity of Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium

All present enzymatic activity of Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium:
3.6.3.8;

Protein crystallography data

The structure of Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium, PDB code: 2zbf was solved by C.Toyoshima, H.Ogawa, Y.Norimatsu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 11.98 / 2.40
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 90.522, 136.473, 106.619, 90.00, 90.00, 90.00
R / Rfree (%) 21.2 / 25.7

Other elements in 2zbf:

The structure of Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium (pdb code 2zbf). 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 Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium, PDB code: 2zbf:

Magnesium binding site 1 out of 1 in 2zbf

Go back to Magnesium Binding Sites List in 2zbf
Magnesium binding site 1 out of 1 in the Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Calcium Pump Crystal Structure with Bound BEF3 and Tg in the Absence of Calcium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg997

b:21.7
occ:1.00
 F2 A:BEF998 1.9 23.5 1.0
O A:HOH2105 2.2 25.5 1.0
OD1 A:ASP351 2.2 17.7 1.0
O A:THR353 2.2 22.6 1.0
OD1 A:ASP703 2.2 24.5 1.0
O A:HOH2114 2.2 19.1 1.0
BE A:BEF998 2.9 28.7 1.0
CG A:ASP351 3.0 20.2 1.0
CG A:ASP703 3.2 27.6 1.0
OD2 A:ASP351 3.3 23.4 1.0
C A:THR353 3.3 20.2 1.0
OD2 A:ASP703 3.5 31.5 1.0
F3 A:BEF998 3.9 25.0 1.0
CB A:THR353 3.9 14.5 1.0
CA A:THR353 3.9 18.4 1.0
F1 A:BEF998 3.9 25.3 1.0
OD2 A:ASP707 3.9 25.4 1.0
O A:SER178 4.1 35.3 1.0
N A:THR353 4.2 19.1 1.0
N A:GLY704 4.2 30.0 1.0
CB A:ASP351 4.4 20.8 1.0
OG1 A:THR355 4.4 22.6 1.0
N A:GLY354 4.5 20.0 1.0
CA A:GLY182 4.5 25.9 1.0
OD1 A:ASN706 4.5 25.2 1.0
CB A:ASP703 4.6 23.9 1.0
CA A:GLY704 4.7 30.4 1.0
CA A:GLY354 4.8 20.4 1.0
CG2 A:THR353 4.8 15.1 1.0
N A:ASP703 4.8 28.1 1.0
C A:LYS352 4.9 20.8 1.0
CG A:ASP707 4.9 25.5 1.0
OG1 A:THR353 5.0 18.5 1.0

Reference:

C.Toyoshima, Y.Norimatsu, S.Iwasawa, T.Tsuda, H.Ogawa. How Processing of Aspartylphosphate Is Coupled to Lumenal Gating of the Ion Pathway in the Calcium Pump Proc.Natl.Acad.Sci.Usa V. 104 19831 2007.
ISSN: ISSN 0027-8424
PubMed: 18077416
DOI: 10.1073/PNAS.0709978104
Page generated: Wed Aug 14 07:49:12 2024

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