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Magnesium in PDB 5lqy: Structure of F-Atpase From Pichia Angusta, in STATE2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of F-Atpase From Pichia Angusta, in STATE2 (pdb code 5lqy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 5 binding sites of Magnesium where determined in the Structure of F-Atpase From Pichia Angusta, in STATE2, PDB code: 5lqy:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5;

Magnesium binding site 1 out of 5 in 5lqy

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Magnesium binding site 1 out of 5 in the Structure of F-Atpase From Pichia Angusta, in STATE2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of F-Atpase From Pichia Angusta, in STATE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:51.0
occ:1.00
O2B A:ATP600 2.4 50.9 1.0
CB A:THR178 3.1 0.0 1.0
PB A:ATP600 3.8 50.9 1.0
O2G A:ATP600 3.9 50.8 0.8
CA A:THR178 4.2 0.0 1.0
N A:THR178 4.2 0.0 1.0
O2A A:ATP600 4.3 45.7 1.0
O3A A:ATP600 4.5 53.2 1.0
O3B A:ATP600 4.5 50.8 1.0
PA A:ATP600 4.9 50.8 1.0
PG A:ATP600 4.9 52.0 0.8
O1B A:ATP600 4.9 52.1 1.0

Magnesium binding site 2 out of 5 in 5lqy

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Magnesium binding site 2 out of 5 in the Structure of F-Atpase From Pichia Angusta, in STATE2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of F-Atpase From Pichia Angusta, in STATE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:40.9
occ:1.00
O3B B:ADP600 2.5 33.8 1.0
CB B:THR178 2.6 0.0 1.0
CA B:THR178 3.7 0.0 1.0
O1A B:ADP600 3.8 33.9 1.0
N B:THR178 3.9 0.0 1.0
PB B:ADP600 4.0 42.6 1.0
O3A B:ADP600 4.5 43.9 1.0
PA B:ADP600 4.5 38.4 1.0
O2A B:ADP600 4.8 29.3 1.0
O1B B:ADP600 4.8 39.6 1.0
O2B B:ADP600 4.9 41.4 1.0
C B:LYS177 5.0 0.0 1.0

Magnesium binding site 3 out of 5 in 5lqy

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Magnesium binding site 3 out of 5 in the Structure of F-Atpase From Pichia Angusta, in STATE2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of F-Atpase From Pichia Angusta, in STATE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:27.9
occ:1.00
O3B C:ADP600 2.5 40.0 1.0
CB C:THR178 2.6 0.0 1.0
CA C:THR178 3.7 0.0 1.0
O1A C:ADP600 3.8 36.2 1.0
N C:THR178 3.8 0.0 1.0
PB C:ADP600 4.0 33.7 1.0
O3A C:ADP600 4.5 35.5 1.0
PA C:ADP600 4.6 39.0 1.0
O1B C:ADP600 4.7 29.8 1.0
O2A C:ADP600 4.8 28.1 1.0
C C:LYS177 4.9 0.0 1.0
O2B C:ADP600 5.0 31.0 1.0

Magnesium binding site 4 out of 5 in 5lqy

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Magnesium binding site 4 out of 5 in the Structure of F-Atpase From Pichia Angusta, in STATE2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of F-Atpase From Pichia Angusta, in STATE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg601

b:35.6
occ:1.00
O3B D:ADP600 2.6 41.6 1.0
CB D:THR165 2.7 0.0 1.0
CA D:THR165 3.6 0.0 1.0
N D:THR165 3.7 0.0 1.0
O1A D:ADP600 3.9 46.7 1.0
PB D:ADP600 4.0 38.9 1.0
O1B D:ADP600 4.6 39.2 1.0
C D:LYS164 4.6 0.0 1.0
O3A D:ADP600 4.7 35.0 1.0
PA D:ADP600 4.8 42.1 1.0
CB D:LYS164 4.9 0.0 1.0
C D:THR165 5.0 0.0 1.0

Magnesium binding site 5 out of 5 in 5lqy

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Magnesium binding site 5 out of 5 in the Structure of F-Atpase From Pichia Angusta, in STATE2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure of F-Atpase From Pichia Angusta, in STATE2 within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg601

b:24.7
occ:1.00
O3B F:ADP600 2.6 27.3 1.0
CB F:THR165 2.8 0.0 1.0
CA F:THR165 3.7 0.0 1.0
N F:THR165 3.7 0.0 1.0
O1A F:ADP600 3.9 31.4 1.0
PB F:ADP600 4.1 26.7 1.0
O1B F:ADP600 4.7 30.5 1.0
C F:LYS164 4.7 0.0 1.0
O3A F:ADP600 4.8 30.2 1.0
PA F:ADP600 4.8 30.1 1.0
CB F:LYS164 4.9 0.0 1.0

Reference:

K.R.Vinothkumar, M.G.Montgomery, S.Liu, J.E.Walker. Structure of the Mitochondrial Atp Synthase Frompichia Angustadetermined By Electron Cryo-Microscopy. Proc. Natl. Acad. Sci. V. 113 12709 2016U.S.A..
ISSN: ESSN 1091-6490
PubMed: 27791192
DOI: 10.1073/PNAS.1615902113
Page generated: Sun Sep 29 20:29:05 2024

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