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Magnesium in PDB 3oeh: Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F

Enzymatic activity of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F

All present enzymatic activity of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F:
3.6.3.14;

Protein crystallography data

The structure of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F, PDB code: 3oeh was solved by D.Arsenieva, J.Symersky, Y.Wang, V.Pagadala, D.M.Mueller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 110.931, 291.896, 188.765, 90.00, 101.91, 90.00
R / Rfree (%) 20.9 / 27

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 15;

Binding sites:

The binding sites of Magnesium atom in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F (pdb code 3oeh). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 15 binding sites of Magnesium where determined in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F, PDB code: 3oeh:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 15 in 3oeh

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Magnesium binding site 1 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


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Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg700

b:41.0
occ:1.00
 O2G A:ANP600 2.2 44.9 1.0
OG1 A:THR178 2.2 55.4 1.0
O2B A:ANP600 2.2 48.6 1.0
CB A:THR178 3.4 50.1 1.0
PB A:ANP600 3.6 51.8 1.0
PG A:ANP600 3.6 48.2 1.0
OD1 A:ASP271 3.8 51.6 1.0
OD2 A:ASP271 3.8 49.3 1.0
N3B A:ANP600 4.1 48.9 1.0
CG A:ASP271 4.2 50.2 1.0
N A:THR178 4.2 49.0 1.0
CA A:THR178 4.3 50.0 1.0
O1B A:ANP600 4.3 49.6 1.0
CG2 A:THR178 4.4 51.0 1.0
O1G A:ANP600 4.5 48.0 1.0
O3G A:ANP600 4.5 48.9 1.0
O3A A:ANP600 4.7 52.1 1.0
O2A A:ANP600 4.9 50.6 1.0

Magnesium binding site 2 out of 15 in 3oeh

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Magnesium binding site 2 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


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Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg700

b:57.9
occ:1.00
 O2B B:ANP600 2.2 67.1 1.0
OG1 B:THR178 2.2 90.0 1.0
O2G B:ANP600 2.2 66.5 1.0
CB B:THR178 3.1 86.2 1.0
PB B:ANP600 3.5 71.5 1.0
PG B:ANP600 3.6 71.5 1.0
OD2 B:ASP271 3.8 72.4 1.0
OD1 B:ASP271 4.0 71.8 1.0
N B:THR178 4.0 85.0 1.0
N3B B:ANP600 4.1 70.5 1.0
CA B:THR178 4.1 86.8 1.0
CG2 B:THR178 4.2 88.3 1.0
O1B B:ANP600 4.2 70.7 1.0
CG B:ASP271 4.3 70.8 1.0
O1G B:ANP600 4.3 71.7 1.0
O2A B:ANP600 4.6 72.5 1.0
O3A B:ANP600 4.7 72.9 1.0
O3G B:ANP600 4.7 71.4 1.0

Magnesium binding site 3 out of 15 in 3oeh

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Magnesium binding site 3 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg700

b:52.1
occ:1.00
 OG1 C:THR178 2.2 73.2 1.0
O2G C:ANP600 2.2 57.5 1.0
O2B C:ANP600 2.2 58.0 1.0
CB C:THR178 3.5 67.5 1.0
PG C:ANP600 3.6 59.6 1.0
PB C:ANP600 3.6 61.6 1.0
OD2 C:ASP271 3.8 64.4 1.0
OD1 C:ASP271 3.9 62.5 1.0
N3B C:ANP600 4.0 60.2 1.0
N C:THR178 4.2 64.4 1.0
CG C:ASP271 4.3 61.6 1.0
O1G C:ANP600 4.3 61.0 1.0
CA C:THR178 4.4 66.7 1.0
CG2 C:THR178 4.4 68.1 1.0
O2A C:ANP600 4.5 63.2 1.0
O1B C:ANP600 4.6 59.6 1.0
O3G C:ANP600 4.6 59.8 1.0
O3A C:ANP600 4.7 62.5 1.0

Magnesium binding site 4 out of 15 in 3oeh

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Magnesium binding site 4 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg700

b:48.7
occ:1.00
 O2B D:ANP600 2.2 55.9 1.0
OG1 D:THR164 2.2 65.2 1.0
O2G D:ANP600 2.2 56.4 1.0
CB D:THR164 2.9 60.4 1.0
OE2 D:GLU193 3.3 62.0 1.0
PG D:ANP600 3.4 57.5 1.0
PB D:ANP600 3.4 57.0 1.0
N3B D:ANP600 3.5 57.2 1.0
O2A D:ANP600 3.7 59.4 1.0
NH1 D:ARG190 3.7 55.9 1.0
CG2 D:THR164 3.8 61.9 1.0
OE1 D:GLU193 3.9 60.4 1.0
CD D:GLU193 3.9 60.7 1.0
O3G D:ANP600 4.0 56.4 1.0
CA D:THR164 4.1 59.9 1.0
N D:THR164 4.2 57.8 1.0
O3A D:ANP600 4.3 58.8 1.0
PA D:ANP600 4.3 58.6 1.0
OE1 D:GLU189 4.5 61.4 1.0
O1B D:ANP600 4.5 57.2 1.0
O1G D:ANP600 4.6 57.0 1.0
O1A D:ANP600 4.6 59.1 1.0
OD2 D:ASP256 4.6 55.2 1.0
NH1 C:ARG375 4.8 67.4 1.0
CZ D:ARG190 5.0 56.0 1.0

Magnesium binding site 5 out of 15 in 3oeh

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Magnesium binding site 5 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg700

b:55.8
occ:1.00
 O2G F:ANP600 2.2 65.4 1.0
OG1 F:THR164 2.2 88.2 1.0
O2B F:ANP600 2.2 66.2 1.0
PG F:ANP600 3.2 70.2 1.0
NH1 F:ARG190 3.2 72.5 1.0
OE2 F:GLU193 3.2 82.8 1.0
CB F:THR164 3.3 82.4 1.0
PB F:ANP600 3.4 70.8 1.0
N3B F:ANP600 3.4 70.0 1.0
OE1 F:GLU193 3.7 82.1 1.0
O3G F:ANP600 3.9 70.6 1.0
OE1 F:GLU189 3.9 77.9 1.0
CD F:GLU193 3.9 82.6 1.0
O2A F:ANP600 4.1 71.6 1.0
CG2 F:THR164 4.1 85.0 1.0
O1B F:ANP600 4.4 71.0 1.0
CD F:GLU189 4.4 76.0 1.0
N F:THR164 4.4 78.3 1.0
CA F:THR164 4.5 81.8 1.0
CZ F:ARG190 4.5 71.4 1.0
O1G F:ANP600 4.5 70.3 1.0
O3A F:ANP600 4.6 71.4 1.0
OD2 F:ASP256 4.8 79.9 1.0
PA F:ANP600 4.8 71.8 1.0
OD1 F:ASP256 4.9 77.4 1.0
CG F:GLU189 4.9 74.0 1.0
NH1 B:ARG375 4.9 84.2 1.0
NH2 F:ARG190 5.0 70.2 1.0

Magnesium binding site 6 out of 15 in 3oeh

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Magnesium binding site 6 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg700

b:51.4
occ:1.00
 OG1 J:THR178 2.2 82.6 1.0
O2B J:ANP600 2.2 60.9 1.0
O2G J:ANP600 2.2 60.0 1.0
CB J:THR178 3.5 77.7 1.0
OD1 J:ASP271 3.5 70.7 1.0
PB J:ANP600 3.5 64.0 1.0
PG J:ANP600 3.6 61.8 1.0
OD2 J:ASP271 3.8 74.2 1.0
CG J:ASP271 4.0 71.9 1.0
N3B J:ANP600 4.1 62.4 1.0
O1B J:ANP600 4.1 63.0 1.0
N J:THR178 4.2 76.0 1.0
CA J:THR178 4.3 78.2 1.0
O1G J:ANP600 4.3 61.5 1.0
CG2 J:THR178 4.4 79.5 1.0
O3G J:ANP600 4.7 62.3 1.0
O3A J:ANP600 4.7 66.9 1.0

Magnesium binding site 7 out of 15 in 3oeh

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Magnesium binding site 7 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Mg700

b:66.1
occ:1.00
 OG1 K:THR178 2.2 0.8 1.0
O2G K:ANP600 2.2 79.1 1.0
O2B K:ANP600 2.2 80.3 1.0
PG K:ANP600 3.5 83.0 1.0
CB K:THR178 3.5 1.0 1.0
PB K:ANP600 3.6 86.9 1.0
OD1 K:ASP271 3.6 0.7 1.0
OD2 K:ASP271 3.9 0.9 1.0
O1G K:ANP600 4.0 82.7 1.0
N3B K:ANP600 4.1 83.5 1.0
CG K:ASP271 4.1 0.7 1.0
CG2 K:THR178 4.2 0.6 1.0
O1B K:ANP600 4.2 87.5 1.0
N K:THR178 4.5 0.7 1.0
CA K:THR178 4.6 0.3 1.0
O3G K:ANP600 4.7 81.7 1.0
O2A K:ANP600 4.8 89.7 1.0
O3A K:ANP600 4.9 88.7 1.0
CD K:GLN210 4.9 0.1 1.0
OE1 K:GLN210 5.0 0.2 1.0
NE2 K:GLN210 5.0 0.2 1.0

Magnesium binding site 8 out of 15 in 3oeh

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Magnesium binding site 8 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Mg700

b:48.2
occ:1.00
 O2G L:ANP600 2.2 49.1 1.0
OG1 L:THR178 2.2 65.8 1.0
O2B L:ANP600 2.2 54.0 1.0
CB L:THR178 3.0 60.3 1.0
PG L:ANP600 3.5 51.4 1.0
PB L:ANP600 3.5 55.0 1.0
N3B L:ANP600 3.8 53.5 1.0
CG2 L:THR178 3.9 61.1 1.0
OD2 L:ASP271 4.0 56.2 1.0
N L:THR178 4.1 59.0 1.0
O2A L:ANP600 4.2 58.2 1.0
CA L:THR178 4.2 60.2 1.0
O3G L:ANP600 4.2 51.7 1.0
O3A L:ANP600 4.3 57.5 1.0
OD1 L:ASP271 4.5 57.0 1.0
PA L:ANP600 4.6 57.5 1.0
O1G L:ANP600 4.6 51.5 1.0
CG L:ASP271 4.7 55.0 1.0
O1B L:ANP600 4.7 53.4 1.0
O1A L:ANP600 4.8 57.7 1.0

Magnesium binding site 9 out of 15 in 3oeh

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Magnesium binding site 9 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
M:Mg700

b:53.4
occ:1.00
 O2G M:ANP600 2.2 63.3 1.0
OG1 M:THR164 2.2 75.8 1.0
O2B M:ANP600 2.2 60.8 1.0
CB M:THR164 3.4 69.8 1.0
OE1 M:GLU189 3.4 71.5 1.0
OD1 M:ASP256 3.6 65.5 1.0
PG M:ANP600 3.6 65.3 1.0
PB M:ANP600 3.6 64.4 1.0
N M:THR164 3.8 68.5 1.0
OD2 M:ASP256 3.9 68.3 1.0
CA M:THR164 4.1 69.9 1.0
CG M:ASP256 4.2 66.5 1.0
CD M:GLU189 4.2 68.7 1.0
O1G M:ANP600 4.2 66.5 1.0
N3B M:ANP600 4.2 63.8 1.0
NH1 M:ARG190 4.3 65.0 1.0
CE M:LYS163 4.5 61.2 1.0
OE1 M:GLU193 4.5 67.4 1.0
O1B M:ANP600 4.5 64.0 1.0
CG2 M:THR164 4.5 71.3 1.0
CB M:LYS163 4.5 65.2 1.0
O3G M:ANP600 4.7 65.3 1.0
O3A M:ANP600 4.7 66.0 1.0
C M:LYS163 4.8 68.1 1.0
O1A M:ANP600 4.8 68.1 1.0
OE2 M:GLU189 4.9 68.8 1.0
CG M:GLU189 4.9 63.8 1.0
OE2 M:GLU193 4.9 70.5 1.0
O2A M:ANP600 5.0 66.3 1.0

Magnesium binding site 10 out of 15 in 3oeh

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Magnesium binding site 10 out of 15 in the Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Structure of Four Mutant Forms of Yeast F1 Atpase: Beta-V279F within 5.0Å range:
probe atom residue distance (Å) B Occ
O:Mg700

b:61.7
occ:1.00
 O2G O:ANP600 2.2 71.1 1.0
OG1 O:THR164 2.2 0.3 1.0
O2B O:ANP600 2.2 69.4 1.0
OE1 O:GLU189 3.4 90.7 1.0
PB O:ANP600 3.4 73.2 1.0
PG O:ANP600 3.5 74.5 1.0
CB O:THR164 3.6 95.4 1.0
OD1 O:ASP256 3.8 83.2 1.0
N O:THR164 3.8 89.3 1.0
N3B O:ANP600 3.9 72.7 1.0
O1B O:ANP600 4.0 72.7 1.0
OD2 O:ASP256 4.0 87.8 1.0
O1G O:ANP600 4.1 75.1 1.0
CA O:THR164 4.1 93.2 1.0
CE O:LYS163 4.1 76.0 1.0
NZ O:LYS163 4.3 76.8 1.0
CD O:GLU189 4.3 87.6 1.0
CB O:LYS163 4.3 80.9 1.0
CG O:ASP256 4.4 83.9 1.0
CG2 O:THR164 4.4 98.3 1.0
NH1 O:ARG190 4.5 92.0 1.0
OE1 O:GLU193 4.5 95.1 1.0
OE2 O:GLU193 4.5 97.9 1.0
C O:LYS163 4.7 86.5 1.0
O3G O:ANP600 4.7 74.9 1.0
O3A O:ANP600 4.7 74.8 1.0
CD O:GLU193 4.9 97.1 1.0

Reference:

D.Arsenieva, J.Symersky, Y.Wang, V.Pagadala, D.M.Mueller. Crystal Structures of Mutant Forms of the Yeast F1 Atpase Reveal Two Modes of Uncoupling. J.Biol.Chem. V. 285 36561 2010.
ISSN: ISSN 0021-9258
PubMed: 20843806
DOI: 10.1074/JBC.M110.174383
Page generated: Thu Aug 15 08:18:29 2024

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