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Magnesium in PDB 7yry: F1-Atpase of Acinetobacter Baumannii

Enzymatic activity of F1-Atpase of Acinetobacter Baumannii

All present enzymatic activity of F1-Atpase of Acinetobacter Baumannii:
7.1.2.2;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the F1-Atpase of Acinetobacter Baumannii (pdb code 7yry). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the F1-Atpase of Acinetobacter Baumannii, PDB code: 7yry:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 7yry

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Magnesium binding site 1 out of 4 in the F1-Atpase of Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of F1-Atpase of Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:39.2
occ:1.00
OG1 A:THR177 2.1 56.2 1.0
O2G A:ATP601 2.2 61.7 1.0
O2B A:ATP601 2.3 66.0 1.0
CB A:THR177 3.3 40.3 1.0
PG A:ATP601 3.5 62.9 1.0
PB A:ATP601 3.6 65.3 1.0
O3B A:ATP601 3.7 59.1 1.0
O1A A:ATP601 4.1 60.9 1.0
CG2 A:THR177 4.1 35.4 1.0
O1G A:ATP601 4.3 67.2 1.0
N A:THR177 4.3 40.9 1.0
OD1 A:ASP262 4.4 50.5 1.0
CA A:THR177 4.4 39.0 1.0
O3A A:ATP601 4.6 59.7 1.0
O1B A:ATP601 4.6 56.8 1.0
O3G A:ATP601 4.6 59.8 1.0
OD2 A:ASP262 4.7 55.5 1.0
PA A:ATP601 4.9 64.9 1.0
CG A:ASP262 5.0 49.5 1.0

Magnesium binding site 2 out of 4 in 7yry

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Magnesium binding site 2 out of 4 in the F1-Atpase of Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of F1-Atpase of Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg602

b:127.5
occ:1.00
O2G B:ATP601 2.0 130.3 1.0
O3B B:ATP601 2.5 133.2 1.0
PG B:ATP601 2.6 135.0 1.0
O1G B:ATP601 3.1 133.8 1.0
OG1 B:THR177 3.4 78.9 1.0
O1A B:ATP601 3.4 135.2 1.0
O2B B:ATP601 3.6 132.4 1.0
PB B:ATP601 3.7 134.2 1.0
CB B:THR177 3.9 76.6 1.0
O3G B:ATP601 4.1 134.9 1.0
PA B:ATP601 4.1 139.3 1.0
O3A B:ATP601 4.1 132.7 1.0
O2A B:ATP601 4.2 133.4 1.0
CG2 B:THR177 4.7 73.7 1.0
NH2 E:ARG347 4.7 134.9 1.0
O1B B:ATP601 4.9 132.6 1.0
N B:THR177 5.0 82.8 1.0

Magnesium binding site 3 out of 4 in 7yry

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Magnesium binding site 3 out of 4 in the F1-Atpase of Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of F1-Atpase of Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:39.6
occ:1.00
O2B C:ATP602 2.1 55.7 1.0
OG1 C:THR177 2.3 55.2 1.0
O2G C:ATP602 2.9 52.2 1.0
PB C:ATP602 3.3 48.0 1.0
O3B C:ATP602 3.4 55.2 1.0
CB C:THR177 3.5 39.7 1.0
PG C:ATP602 3.5 60.3 1.0
O1G C:ATP602 3.8 60.3 1.0
CG2 C:THR177 4.1 34.6 1.0
O1A C:ATP602 4.2 60.6 1.0
O3A C:ATP602 4.2 43.0 1.0
OD1 C:ASP262 4.3 62.6 1.0
O1B C:ATP602 4.3 49.7 1.0
PA C:ATP602 4.6 44.4 1.0
N C:THR177 4.6 36.9 1.0
CA C:THR177 4.6 30.7 1.0
O2A C:ATP602 4.7 56.8 1.0
O3G C:ATP602 5.0 58.6 1.0

Magnesium binding site 4 out of 4 in 7yry

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Magnesium binding site 4 out of 4 in the F1-Atpase of Acinetobacter Baumannii


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of F1-Atpase of Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg501

b:80.2
occ:1.00
O3B D:ADP502 2.2 64.9 1.0
O1B D:ADP502 2.3 53.4 1.0
PB D:ADP502 2.4 69.4 1.0
NZ D:LYS154 2.7 41.6 1.0
O2B D:ADP502 3.1 54.5 1.0
CE D:LYS154 3.3 31.9 1.0
O D:GLY149 3.9 52.1 1.0
O3A D:ADP502 4.0 55.4 1.0
N D:GLY151 4.0 40.0 1.0
CB D:LYS154 4.3 37.3 1.0
CG D:LYS154 4.4 35.9 1.0
CA D:ALA150 4.5 50.7 1.0
CD D:LYS154 4.5 32.2 1.0
C D:ALA150 4.7 51.8 1.0
OG1 D:THR155 4.8 56.2 1.0
NH1 A:ARG377 4.8 50.0 1.0
N D:LYS154 4.8 39.3 1.0
CA D:GLY151 4.9 39.9 1.0
C D:GLY149 4.9 43.6 1.0
O1A D:ADP502 4.9 59.8 1.0

Reference:

W.G.Saw, K.C.M.Le, J.Shi, J.H.M.Kwek, C.F.Wong, P.Ragunathan, T.C.Fong, V.Muller, G.Grueber. Atomic Insights of An Up and Down Conformation of the Acinetobacter Baumannii F1-Atpase Subunit Epsilon and Deciphering the Residues Critical For Atp Hydrolysis Inhibition and Atp Synthesis. Faseb J. V. 37 2023.
ISSN: ESSN 1530-6860
DOI: 10.1096/FJ.202300175RR
Page generated: Thu Oct 3 15:40:04 2024

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