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Magnesium in PDB 2xnd: Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase

Enzymatic activity of Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase

All present enzymatic activity of Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase:
3.6.3.14;

Protein crystallography data

The structure of Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase, PDB code: 2xnd was solved by I.N.Watt, M.G.Montgomery, M.J.Runswick, A.G.W.Leslie, J.E.Walker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 132.60 / 3.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 155.740, 157.100, 247.270, 90.00, 90.00, 90.00
R / Rfree (%) 26.126 / 30.397

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase (pdb code 2xnd). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase, PDB code: 2xnd:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 2xnd

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Magnesium binding site 1 out of 5 in the Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase


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 Bovine F1-C8 Sub-Complex of Atp Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:43.9
occ:1.00
OG1 A:THR176 2.2 49.2 1.0
O2G A:ANP600 2.3 43.3 1.0
O2B A:ANP600 2.3 43.5 1.0
CB A:THR176 3.5 50.8 1.0
OD2 A:ASP269 3.7 59.0 1.0
PB A:ANP600 3.7 42.5 1.0
PG A:ANP600 3.7 42.7 1.0
OD1 A:ASP269 3.8 59.1 1.0
N3B A:ANP600 4.1 42.7 1.0
CG A:ASP269 4.1 58.9 1.0
O1B A:ANP600 4.2 42.4 1.0
O3G A:ANP600 4.3 42.2 1.0
NE2 A:GLN208 4.3 60.8 1.0
CG2 A:THR176 4.4 50.8 1.0
N A:THR176 4.4 51.1 1.0
CA A:THR176 4.5 50.9 1.0
O2A A:ANP600 4.7 41.9 1.0
O1G A:ANP600 4.9 42.6 1.0
O3A A:ANP600 4.9 42.1 1.0

Magnesium binding site 2 out of 5 in 2xnd

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Magnesium binding site 2 out of 5 in the Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase


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 Bovine F1-C8 Sub-Complex of Atp Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:55.1
occ:1.00
O2G B:ANP600 2.1 55.1 1.0
OG1 B:THR176 2.2 54.5 1.0
O2B B:ANP600 2.3 54.8 1.0
PG B:ANP600 3.0 54.8 1.0
O2A B:ANP600 3.1 57.3 1.0
N3B B:ANP600 3.1 54.8 1.0
CB B:THR176 3.2 54.3 1.0
PB B:ANP600 3.2 54.6 1.0
O1G B:ANP600 3.5 54.6 1.0
CG2 B:THR176 4.0 54.2 1.0
PA B:ANP600 4.0 56.9 1.0
O3A B:ANP600 4.1 55.7 1.0
OD2 B:ASP269 4.2 54.9 1.0
O1A B:ANP600 4.3 56.8 1.0
O3G B:ANP600 4.4 54.9 1.0
CA B:THR176 4.4 54.2 1.0
N B:THR176 4.4 53.9 1.0
O1B B:ANP600 4.5 55.3 1.0

Magnesium binding site 3 out of 5 in 2xnd

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Magnesium binding site 3 out of 5 in the Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:60.8
occ:1.00
OG1 C:THR176 2.1 63.5 1.0
O2G C:ANP600 2.2 60.1 1.0
O2B C:ANP600 2.2 60.7 1.0
CB C:THR176 3.0 64.6 1.0
PG C:ANP600 3.5 60.0 1.0
PB C:ANP600 3.5 60.8 1.0
OD2 C:ASP269 3.6 58.2 1.0
N3B C:ANP600 3.7 60.4 1.0
CG2 C:THR176 3.8 64.6 1.0
OD1 C:ASP269 4.2 58.5 1.0
O2A C:ANP600 4.2 60.8 1.0
CA C:THR176 4.3 64.7 1.0
N C:THR176 4.3 64.5 1.0
CG C:ASP269 4.3 58.2 1.0
O3G C:ANP600 4.4 59.6 1.0
O1A C:ANP600 4.5 61.0 1.0
O3A C:ANP600 4.5 60.9 1.0
O1G C:ANP600 4.6 60.2 1.0
PA C:ANP600 4.6 60.9 1.0
O1B C:ANP600 4.6 61.0 1.0

Magnesium binding site 4 out of 5 in 2xnd

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Magnesium binding site 4 out of 5 in the Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg601

b:62.1
occ:1.00
OG1 D:THR163 2.0 58.1 1.0
O2G D:ANP600 2.2 66.8 1.0
O2B D:ANP600 2.2 63.5 1.0
OE1 D:GLU188 2.9 72.9 1.0
CB D:THR163 3.5 57.4 1.0
PB D:ANP600 3.6 64.3 1.0
PG D:ANP600 3.6 68.2 1.0
CD D:GLU188 3.6 72.4 1.0
OD1 D:ASP256 3.7 56.3 1.0
OD2 D:ASP256 3.8 55.8 1.0
N3B D:ANP600 4.0 66.0 1.0
N D:THR163 4.1 57.0 1.0
CE D:LYS162 4.1 54.9 1.0
NH1 D:ARG189 4.1 74.6 1.0
CG D:GLU188 4.1 71.3 1.0
CG2 D:THR163 4.2 57.6 1.0
OE1 D:GLU192 4.2 70.9 1.0
CG D:ASP256 4.2 56.1 1.0
OE2 D:GLU192 4.2 70.7 1.0
CA D:THR163 4.3 57.5 1.0
O1B D:ANP600 4.4 64.1 1.0
O1G D:ANP600 4.4 67.5 1.0
OE2 D:GLU188 4.5 72.6 1.0
NZ D:LYS162 4.6 54.7 1.0
NH1 C:ARG373 4.6 68.9 1.0
CB D:LYS162 4.6 56.0 1.0
O2A D:ANP600 4.6 63.6 1.0
CD D:GLU192 4.6 70.8 1.0
O3G D:ANP600 4.7 67.9 1.0
O3A D:ANP600 4.8 64.2 1.0
O1A D:ANP600 5.0 64.0 1.0
CB D:GLU188 5.0 70.4 1.0

Magnesium binding site 5 out of 5 in 2xnd

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Magnesium binding site 5 out of 5 in the Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Bovine F1-C8 Sub-Complex of Atp Synthase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg601

b:57.0
occ:1.00
O2G F:ANP600 2.1 56.1 1.0
O2B F:ANP600 2.2 57.0 1.0
OG1 F:THR163 2.2 56.3 1.0
CB F:THR163 2.9 56.5 1.0
N3B F:ANP600 2.9 56.0 1.0
PG F:ANP600 3.0 55.5 1.0
PB F:ANP600 3.1 56.9 1.0
O2A F:ANP600 3.2 59.1 1.0
NH1 F:ARG189 3.4 67.6 1.0
OE2 F:GLU192 3.5 70.4 1.0
OE1 F:GLU188 3.5 68.1 1.0
O1G F:ANP600 3.8 55.4 1.0
CG2 F:THR163 3.9 56.3 1.0
PA F:ANP600 3.9 58.7 1.0
O1A F:ANP600 4.0 58.6 1.0
O3A F:ANP600 4.0 57.6 1.0
N F:THR163 4.0 56.2 1.0
CA F:THR163 4.1 56.5 1.0
O3G F:ANP600 4.3 56.1 1.0
OE1 F:GLU192 4.3 70.7 1.0
CD F:GLU192 4.3 70.6 1.0
O1B F:ANP600 4.4 57.7 1.0
NH1 B:ARG373 4.4 73.6 1.0
CD F:GLU188 4.5 68.1 1.0
CZ F:ARG189 4.6 67.7 1.0
OD2 F:ASP256 4.7 58.1 1.0
NH2 F:ARG189 5.0 67.4 1.0

Reference:

I.N.Watt, M.G.Montgomery, M.J.Runswick, A.G.W.Leslie, J.E.Walker. Bioenergetic Cost of Making An Adenosine Triphosphate Molecule in Animal Mitochondria. Proc.Natl.Acad.Sci.Usa V. 107 16823 2010.
ISSN: ISSN 0027-8424
PubMed: 20847295
DOI: 10.1073/PNAS.1011099107
Page generated: Sun Aug 10 16:29:25 2025

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