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Magnesium in PDB 7tju: Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp

Enzymatic activity of Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp

All present enzymatic activity of Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp:
7.1.2.2;

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp (pdb code 7tju). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp, PDB code: 7tju:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 7tju

Go back to Magnesium Binding Sites List in 7tju
Magnesium binding site 1 out of 3 in the Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:48.4
occ:1.00
OG1 A:THR178 2.1 45.0 1.0
O2B A:ATP600 2.1 56.4 1.0
O2G A:ATP600 2.1 56.4 1.0
CB A:THR178 3.0 45.0 1.0
O3B A:ATP600 3.1 56.4 1.0
PB A:ATP600 3.1 56.4 1.0
PG A:ATP600 3.2 56.4 1.0
N A:THR178 3.8 45.0 1.0
OD2 A:ASP271 4.0 35.3 1.0
CA A:THR178 4.0 45.0 1.0
O1A A:ATP600 4.0 56.4 1.0
O3A A:ATP600 4.1 56.4 1.0
CG2 A:THR178 4.1 45.0 1.0
O1G A:ATP600 4.1 56.4 1.0
OD1 A:ASP271 4.2 35.3 1.0
O3G A:ATP600 4.2 56.4 1.0
O1B A:ATP600 4.3 56.4 1.0
PA A:ATP600 4.4 56.4 1.0
O2A A:ATP600 4.5 56.4 1.0
CG A:ASP271 4.5 35.3 1.0
NZ A:LYS177 5.0 47.3 1.0
C A:LYS177 5.0 47.3 1.0

Magnesium binding site 2 out of 3 in 7tju

Go back to Magnesium Binding Sites List in 7tju
Magnesium binding site 2 out of 3 in the Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:33.6
occ:1.00
O2B B:ATP600 2.1 37.7 1.0
OG1 B:THR178 2.1 30.7 1.0
O2G B:ATP600 2.1 37.7 1.0
CB B:THR178 2.9 30.7 1.0
O3B B:ATP600 3.2 37.7 1.0
PB B:ATP600 3.2 37.7 1.0
PG B:ATP600 3.3 37.7 1.0
CG2 B:THR178 3.9 30.7 1.0
OD2 B:ASP271 4.0 25.1 1.0
N B:THR178 4.0 30.7 1.0
CA B:THR178 4.0 30.7 1.0
O3A B:ATP600 4.2 37.7 1.0
O1G B:ATP600 4.2 37.7 1.0
O1A B:ATP600 4.2 37.7 1.0
O1B B:ATP600 4.2 37.7 1.0
O3G B:ATP600 4.3 37.7 1.0
OD1 B:ASP271 4.3 25.1 1.0
NH2 E:ARG356 4.6 37.2 1.0
CG B:ASP271 4.6 25.1 1.0
PA B:ATP600 4.6 37.7 1.0
O2A B:ATP600 4.8 37.7 1.0

Magnesium binding site 3 out of 3 in 7tju

Go back to Magnesium Binding Sites List in 7tju
Magnesium binding site 3 out of 3 in the Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Yeast Atp Synthase F1 Region State 1-3BINDING BETA_TIGHT Open Without Exogenous Atp within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg601

b:30.4
occ:1.00
OG1 C:THR178 2.1 28.1 1.0
O2B C:ATP600 2.1 32.9 1.0
O3G C:ATP600 2.1 32.9 1.0
CB C:THR178 3.0 28.1 1.0
O3B C:ATP600 3.2 32.9 1.0
PB C:ATP600 3.2 32.9 1.0
PG C:ATP600 3.2 32.9 1.0
OD2 C:ASP271 3.8 24.6 1.0
N C:THR178 3.9 28.1 1.0
OD1 C:ASP271 4.0 24.6 1.0
CA C:THR178 4.1 28.1 1.0
O1G C:ATP600 4.1 32.9 1.0
CG2 C:THR178 4.1 28.1 1.0
O1B C:ATP600 4.2 32.9 1.0
O3A C:ATP600 4.3 32.9 1.0
O2G C:ATP600 4.3 32.9 1.0
CG C:ASP271 4.4 24.6 1.0
O1A C:ATP600 4.4 32.9 1.0
PA C:ATP600 4.8 32.9 1.0
NZ C:LYS177 4.9 28.8 1.0
O2A C:ATP600 5.0 32.9 1.0

Reference:

H.Guo, J.L.Rubinstein. Structure of Atp Synthase Under Strain During Catalysis. Nat Commun V. 13 2232 2022.
ISSN: ESSN 2041-1723
PubMed: 35468906
DOI: 10.1038/S41467-022-29893-2
Page generated: Thu Oct 3 09:19:16 2024

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