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Magnesium in PDB 3eya: Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli

Enzymatic activity of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli

All present enzymatic activity of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli:
1.2.2.2;

Protein crystallography data

The structure of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli, PDB code: 3eya was solved by P.Neumann, A.Weidner, A.Pech, M.T.Stubbs, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 203.243, 207.051, 214.542, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 19.8

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Magnesium atom in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli (pdb code 3eya). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli, PDB code: 3eya:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 12 in 3eya

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Magnesium binding site 1 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


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Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg613

b:52.7
occ:1.00
 O23 A:TDP611 1.9 49.0 1.0
OD1 A:ASP433 1.9 52.8 1.0
O A:VAL462 2.1 47.9 0.5
OD1 A:ASN460 2.1 52.8 1.0
O12 A:TDP611 2.2 49.2 1.0
CG A:ASN460 3.1 51.7 1.0
P2 A:TDP611 3.1 48.4 1.0
CG A:ASP433 3.1 53.0 1.0
P1 A:TDP611 3.2 47.9 1.0
C A:VAL462 3.3 51.6 0.5
ND2 A:ASN460 3.4 50.2 1.0
O22 A:TDP611 3.4 47.8 1.0
O11 A:TDP611 3.5 46.2 1.0
OD2 A:ASP433 3.7 56.9 1.0
N A:ASP433 3.9 47.6 1.0
N A:VAL462 4.0 55.2 0.5
N A:GLY464 4.0 52.9 0.5
O5G A:TDP611 4.1 50.1 1.0
O A:PHE458 4.1 49.8 1.0
CA A:VAL462 4.2 53.5 0.5
N A:LEU463 4.2 52.5 0.5
N A:GLY434 4.3 46.9 1.0
CG1 A:VAL462 4.3 52.8 0.5
CA A:LEU463 4.3 51.5 0.5
CB A:ASP433 4.4 51.0 1.0
N A:ASN460 4.4 52.0 1.0
CB A:ASN460 4.4 53.1 1.0
O21 A:TDP611 4.4 47.1 1.0
O13 A:TDP611 4.5 49.7 1.0
CA A:ASP433 4.6 48.7 1.0
CA A:GLY432 4.7 46.4 1.0
C A:LEU463 4.7 52.6 0.5
CA A:ASN460 4.8 53.6 1.0
N A:SER461 4.8 56.1 1.0
C A:GLY432 4.8 47.5 1.0
C A:ASN460 4.8 55.3 1.0
CA A:GLY464 4.9 55.6 0.5
CB A:VAL462 4.9 54.4 0.5
C A:ASP433 5.0 48.5 1.0

Magnesium binding site 2 out of 12 in 3eya

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Magnesium binding site 2 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


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Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg613

b:55.8
occ:1.00
 OD1 B:ASP433 2.0 57.6 1.0
O12 B:TDP611 2.1 54.9 1.0
OD1 B:ASN460 2.2 59.1 1.0
O23 B:TDP611 2.2 58.8 1.0
O B:VAL462 2.3 52.6 0.5
O22 B:TDP611 3.0 54.9 1.0
P2 B:TDP611 3.0 55.2 1.0
CG B:ASN460 3.0 59.3 1.0
CG B:ASP433 3.2 57.2 1.0
P1 B:TDP611 3.2 52.0 1.0
ND2 B:ASN460 3.3 58.0 1.0
O11 B:TDP611 3.4 53.6 1.0
C B:VAL462 3.5 56.5 0.5
OD2 B:ASP433 3.8 60.8 1.0
N B:ASP433 3.9 52.6 1.0
O B:PHE458 4.0 56.9 1.0
O5G B:TDP611 4.1 52.0 1.0
N B:GLY464 4.1 58.9 0.5
N B:VAL462 4.2 60.2 0.5
N B:GLY434 4.3 50.5 1.0
O13 B:TDP611 4.4 52.7 1.0
CB B:ASP433 4.4 55.2 1.0
O21 B:TDP611 4.4 54.2 1.0
N B:LEU463 4.4 56.8 0.5
N B:ASN460 4.4 58.9 1.0
CA B:VAL462 4.4 58.7 0.5
CB B:ASN460 4.4 61.4 1.0
CG1 B:VAL462 4.5 59.6 0.5
CA B:LEU463 4.5 55.8 0.5
CA B:GLY432 4.6 52.2 1.0
CA B:ASP433 4.6 52.7 1.0
C B:GLY432 4.7 52.4 1.0
CA B:ASN460 4.8 61.6 1.0
C B:LEU463 4.9 57.9 0.5
C B:ASN460 4.9 62.2 1.0
N B:SER461 4.9 62.1 1.0
CA B:GLY464 5.0 62.6 0.5
C B:ASP433 5.0 52.0 1.0

Magnesium binding site 3 out of 12 in 3eya

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Magnesium binding site 3 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg613

b:63.4
occ:1.00
 O23 C:TDP611 1.9 54.8 1.0
OD1 C:ASP433 2.0 60.6 1.0
O C:VAL462 2.1 55.9 0.5
OD1 C:ASN460 2.2 61.2 1.0
O12 C:TDP611 2.2 49.6 1.0
P2 C:TDP611 3.0 54.0 1.0
CG C:ASN460 3.1 60.5 1.0
CG C:ASP433 3.2 60.7 1.0
P1 C:TDP611 3.2 49.6 1.0
ND2 C:ASN460 3.3 59.0 1.0
C C:VAL462 3.3 60.0 0.5
O22 C:TDP611 3.4 54.9 1.0
O11 C:TDP611 3.4 50.6 1.0
OD2 C:ASP433 3.8 64.8 1.0
N C:ASP433 3.9 54.7 1.0
O5G C:TDP611 4.0 49.9 1.0
N C:GLY464 4.0 61.4 0.5
N C:VAL462 4.1 64.1 0.5
O C:PHE458 4.1 58.0 1.0
N C:LEU463 4.3 60.7 0.5
CA C:VAL462 4.3 62.5 0.5
N C:GLY434 4.3 53.7 1.0
O21 C:TDP611 4.3 53.3 1.0
CA C:LEU463 4.4 59.4 0.5
CG1 C:VAL462 4.4 62.3 0.5
O13 C:TDP611 4.4 50.4 1.0
CB C:ASP433 4.4 58.5 1.0
CB C:ASN460 4.5 62.7 1.0
N C:ASN460 4.5 60.7 1.0
CA C:GLY432 4.7 53.1 1.0
CA C:ASP433 4.7 55.5 1.0
C C:LEU463 4.7 60.8 0.5
C C:GLY432 4.8 54.0 1.0
CD1 C:LEU482 4.8 56.1 0.5
CA C:ASN460 4.8 63.4 1.0
N C:SER461 4.9 65.2 1.0
CA C:GLY464 4.9 64.5 0.5
C C:ASN460 4.9 64.7 1.0
CB C:VAL462 5.0 64.0 0.5

Magnesium binding site 4 out of 12 in 3eya

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Magnesium binding site 4 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


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Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg613

b:57.6
occ:1.00
 OD1 D:ASN460 2.0 56.0 1.0
OD1 D:ASP433 2.0 56.0 1.0
O23 D:TDP611 2.1 50.2 1.0
O D:VAL462 2.1 50.6 0.5
O12 D:TDP611 2.3 50.2 1.0
CG D:ASN460 2.9 54.9 1.0
P2 D:TDP611 3.0 48.2 1.0
ND2 D:ASN460 3.2 53.4 1.0
CG D:ASP433 3.2 56.3 1.0
P1 D:TDP611 3.3 47.7 1.0
C D:VAL462 3.3 54.4 0.5
O11 D:TDP611 3.3 48.0 1.0
O22 D:TDP611 3.3 48.0 1.0
OD2 D:ASP433 3.7 60.1 1.0
N D:GLY464 4.0 55.4 0.5
N D:ASP433 4.0 51.0 1.0
N D:VAL462 4.0 58.4 0.5
O D:PHE458 4.1 53.4 1.0
O5G D:TDP611 4.1 50.1 1.0
CA D:VAL462 4.2 56.5 0.5
CG1 D:VAL462 4.3 55.6 0.5
N D:LEU463 4.3 54.9 0.5
CB D:ASN460 4.3 56.6 1.0
N D:ASN460 4.4 55.8 1.0
CA D:LEU463 4.4 53.8 0.5
N D:GLY434 4.4 50.2 1.0
O21 D:TDP611 4.4 49.7 1.0
CB D:ASP433 4.5 54.9 1.0
O13 D:TDP611 4.5 49.3 1.0
CA D:ASN460 4.7 57.7 1.0
CA D:ASP433 4.7 51.9 1.0
N D:SER461 4.7 59.7 1.0
CA D:GLY432 4.7 49.8 1.0
C D:ASN460 4.8 59.0 1.0
C D:LEU463 4.8 54.8 0.5
CA D:GLY464 4.9 58.1 0.5
C D:GLY432 4.9 51.0 1.0
CB D:VAL462 4.9 57.3 0.5

Magnesium binding site 5 out of 12 in 3eya

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Magnesium binding site 5 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg613

b:70.3
occ:1.00
 OD1 E:ASP433 1.9 80.4 1.0
O12 E:TDP611 2.0 66.6 1.0
O23 E:TDP611 2.1 67.7 1.0
OD1 E:ASN460 2.3 83.1 1.0
O E:VAL462 2.4 76.5 0.5
P2 E:TDP611 2.9 67.1 1.0
O22 E:TDP611 2.9 65.7 1.0
P1 E:TDP611 3.1 64.4 1.0
CG E:ASN460 3.1 83.3 1.0
CG E:ASP433 3.2 80.8 1.0
O11 E:TDP611 3.3 65.0 1.0
ND2 E:ASN460 3.4 81.4 1.0
C E:VAL462 3.7 80.8 0.5
N E:ASP433 3.7 74.0 1.0
OD2 E:ASP433 3.8 85.5 1.0
O E:PHE458 3.9 79.1 1.0
O13 E:TDP611 4.1 64.1 1.0
O5G E:TDP611 4.2 64.7 1.0
N E:GLY434 4.2 71.6 1.0
N E:GLY464 4.3 81.7 0.5
CB E:ASP433 4.3 78.7 1.0
O21 E:TDP611 4.3 65.4 1.0
CA E:GLY432 4.3 71.6 1.0
N E:VAL462 4.3 86.4 0.5
N E:ASN460 4.4 84.2 1.0
CA E:ASP433 4.5 74.9 1.0
C E:GLY432 4.5 72.5 1.0
CB E:ASN460 4.5 86.6 1.0
N E:LEU463 4.6 81.0 0.5
CA E:VAL462 4.6 84.5 0.5
CA E:LEU463 4.6 78.9 0.5
CG1 E:VAL462 4.7 85.1 0.5
CA E:ASN460 4.9 87.4 1.0
C E:ASP433 4.9 73.5 1.0
N E:SER461 5.0 88.5 1.0

Magnesium binding site 6 out of 12 in 3eya

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Magnesium binding site 6 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg613

b:76.7
occ:1.00
 O12 F:TDP611 2.1 62.6 1.0
O23 F:TDP611 2.1 65.2 1.0
OD1 F:ASP433 2.1 77.4 1.0
OD1 F:ASN460 2.2 79.2 1.0
O F:VAL462 2.3 72.6 0.5
O22 F:TDP611 2.9 63.8 1.0
P2 F:TDP611 2.9 62.9 1.0
CG F:ASN460 3.0 79.0 1.0
ND2 F:ASN460 3.2 77.0 1.0
P1 F:TDP611 3.2 61.7 1.0
O11 F:TDP611 3.3 61.8 1.0
CG F:ASP433 3.3 77.8 1.0
C F:VAL462 3.5 76.8 0.5
OD2 F:ASP433 3.9 82.4 1.0
N F:ASP433 4.0 70.8 1.0
O F:PHE458 4.0 75.6 1.0
N F:GLY464 4.0 77.0 0.5
O5G F:TDP611 4.1 62.8 1.0
N F:VAL462 4.3 82.9 0.5
O21 F:TDP611 4.3 61.9 1.0
CB F:ASN460 4.4 82.0 1.0
O13 F:TDP611 4.4 60.9 1.0
CG1 F:VAL462 4.4 80.5 0.5
N F:LEU463 4.4 76.9 0.5
N F:ASN460 4.4 80.5 1.0
N F:GLY434 4.4 69.0 1.0
CA F:VAL462 4.5 80.5 0.5
CA F:LEU463 4.5 74.6 0.5
CB F:ASP433 4.5 75.9 1.0
CA F:GLY432 4.6 68.5 1.0
CA F:ASP433 4.7 72.1 1.0
C F:GLY432 4.8 69.8 1.0
CA F:ASN460 4.8 83.5 1.0
C F:LEU463 4.8 76.0 0.5
CA F:GLY464 4.9 80.5 0.5
C F:ASN460 4.9 85.0 1.0
N F:SER461 4.9 85.1 1.0

Magnesium binding site 7 out of 12 in 3eya

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Magnesium binding site 7 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg613

b:67.4
occ:1.00
 O23 G:TDP611 2.0 59.2 1.0
OD1 G:ASP433 2.1 76.2 1.0
O12 G:TDP611 2.2 63.5 1.0
OD1 G:ASN460 2.2 78.5 1.0
O G:VAL462 2.5 71.5 0.5
P2 G:TDP611 2.8 59.7 1.0
O22 G:TDP611 2.9 57.5 1.0
CG G:ASN460 3.0 78.2 1.0
ND2 G:ASN460 3.2 76.2 1.0
P1 G:TDP611 3.2 60.1 1.0
O11 G:TDP611 3.3 61.4 1.0
CG G:ASP433 3.3 76.5 1.0
C G:VAL462 3.7 75.5 0.5
N G:ASP433 3.8 70.3 1.0
O G:PHE458 3.9 75.2 1.0
OD2 G:ASP433 3.9 80.6 1.0
O5G G:TDP611 4.0 59.8 1.0
N G:GLY464 4.2 76.5 0.5
O21 G:TDP611 4.2 57.1 1.0
N G:GLY434 4.4 68.0 1.0
N G:VAL462 4.4 80.9 0.5
N G:ASN460 4.4 79.0 1.0
CA G:GLY432 4.4 68.4 1.0
O13 G:TDP611 4.4 62.0 1.0
CB G:ASP433 4.4 74.7 1.0
CB G:ASN460 4.4 81.0 1.0
CG1 G:VAL462 4.6 79.2 0.5
N G:LEU463 4.6 75.5 0.5
C G:GLY432 4.6 69.6 1.0
CA G:VAL462 4.6 78.8 0.5
CA G:ASP433 4.6 71.2 1.0
CA G:LEU463 4.7 73.8 0.5
CA G:ASN460 4.8 82.0 1.0
C G:LEU463 5.0 75.5 0.5
N G:SER461 5.0 83.1 1.0
C G:ASN460 5.0 83.2 1.0

Magnesium binding site 8 out of 12 in 3eya

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Magnesium binding site 8 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg613

b:59.4
occ:1.00
 O H:VAL462 1.8 66.5 0.5
O23 H:TDP611 2.0 58.8 1.0
OD1 H:ASP433 2.1 71.0 1.0
O12 H:TDP611 2.1 59.5 1.0
OD1 H:ASN460 2.2 72.3 1.0
O H:HOH651 2.3 60.6 1.0
C H:VAL462 3.0 70.7 0.5
CG H:ASN460 3.1 71.7 1.0
P2 H:TDP611 3.1 59.2 1.0
CG H:ASP433 3.2 71.8 1.0
P1 H:TDP611 3.2 57.6 1.0
ND2 H:ASN460 3.4 69.5 1.0
O11 H:TDP611 3.5 57.8 1.0
O22 H:TDP611 3.6 57.7 1.0
OD2 H:ASP433 3.7 76.2 1.0
N H:GLY464 3.8 70.5 0.5
N H:VAL462 3.8 76.4 0.5
N H:LEU463 3.9 70.9 0.5
O5G H:TDP611 4.0 59.7 1.0
CA H:VAL462 4.0 74.3 0.5
CA H:LEU463 4.1 68.8 0.5
N H:ASP433 4.1 64.8 1.0
CG1 H:VAL462 4.1 73.6 0.5
N H:GLY434 4.3 63.5 1.0
O H:PHE458 4.4 68.2 1.0
O21 H:TDP611 4.5 59.6 1.0
CB H:ASP433 4.5 70.0 1.0
O13 H:TDP611 4.5 58.2 1.0
CB H:ASN460 4.5 74.6 1.0
C H:LEU463 4.5 69.8 0.5
N H:ASN460 4.6 73.4 1.0
CB H:VAL462 4.7 75.9 0.5
CA H:GLY464 4.8 73.5 0.5
CA H:ASP433 4.8 66.1 1.0
N H:SER461 4.8 78.4 1.0
C H:ASN460 4.8 77.9 1.0
CA H:ASN460 4.8 76.2 1.0
CA H:GLY432 4.9 61.9 1.0
C H:GLY432 5.0 63.3 1.0

Magnesium binding site 9 out of 12 in 3eya

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Magnesium binding site 9 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Mg613

b:62.8
occ:1.00
 OD1 I:ASP433 1.9 70.1 1.0
O I:VAL462 2.0 65.4 0.5
OD1 I:ASN460 2.1 71.7 1.0
O23 I:TDP611 2.1 58.0 1.0
O12 I:TDP611 2.1 56.8 1.0
CG I:ASN460 3.0 71.5 1.0
CG I:ASP433 3.0 70.2 1.0
P2 I:TDP611 3.2 57.6 1.0
C I:VAL462 3.2 69.6 0.5
ND2 I:ASN460 3.3 69.9 1.0
P1 I:TDP611 3.4 56.1 1.0
O22 I:TDP611 3.4 59.9 1.0
OD2 I:ASP433 3.6 74.6 1.0
O11 I:TDP611 3.6 55.7 1.0
N I:VAL462 3.9 74.7 0.5
N I:ASP433 3.9 64.1 1.0
O5G I:TDP611 4.1 55.3 1.0
N I:GLY464 4.1 70.5 0.5
O I:PHE458 4.1 68.4 1.0
CA I:VAL462 4.2 72.7 0.5
N I:LEU463 4.2 69.8 0.5
N I:GLY434 4.3 62.1 1.0
CG1 I:VAL462 4.3 72.9 0.5
CB I:ASP433 4.3 68.2 1.0
N I:ASN460 4.4 72.5 1.0
CA I:LEU463 4.4 68.0 0.5
CB I:ASN460 4.4 74.4 1.0
O21 I:TDP611 4.5 56.6 1.0
CA I:ASP433 4.6 65.0 1.0
O13 I:TDP611 4.6 53.4 1.0
N I:SER461 4.7 76.5 1.0
CA I:ASN460 4.7 75.1 1.0
C I:ASN460 4.7 76.4 1.0
CA I:GLY432 4.7 62.2 1.0
C I:GLY432 4.8 63.3 1.0
C I:LEU463 4.8 69.6 0.5
CB I:VAL462 4.9 74.5 0.5
C I:ASP433 5.0 63.9 1.0
CA I:GLY464 5.0 74.0 0.5

Magnesium binding site 10 out of 12 in 3eya

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Magnesium binding site 10 out of 12 in the Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
J:Mg613

b:72.1
occ:1.00
 OD1 J:ASP433 1.8 73.6 1.0
O12 J:TDP611 2.1 62.6 1.0
O J:VAL462 2.1 69.2 0.5
O23 J:TDP611 2.1 61.9 1.0
OD1 J:ASN460 2.2 76.0 1.0
CG J:ASP433 3.0 73.7 1.0
CG J:ASN460 3.1 75.9 1.0
P2 J:TDP611 3.2 62.7 1.0
P1 J:TDP611 3.3 61.1 1.0
C J:VAL462 3.4 73.0 0.5
ND2 J:ASN460 3.4 74.2 1.0
O22 J:TDP611 3.4 63.5 1.0
O11 J:TDP611 3.5 60.7 1.0
OD2 J:ASP433 3.6 78.0 1.0
N J:ASP433 3.8 67.6 1.0
N J:VAL462 4.0 78.0 0.5
O J:PHE458 4.1 72.2 1.0
O5G J:TDP611 4.1 62.1 1.0
N J:GLY464 4.2 74.5 0.5
N J:GLY434 4.2 65.2 1.0
CB J:ASP433 4.2 71.3 1.0
CA J:VAL462 4.3 76.0 0.5
N J:LEU463 4.3 73.2 0.5
O13 J:TDP611 4.4 60.6 1.0
N J:ASN460 4.4 76.3 1.0
CA J:LEU463 4.4 71.5 0.5
CG1 J:VAL462 4.4 76.7 0.5
CA J:ASP433 4.5 68.0 1.0
CB J:ASN460 4.5 78.6 1.0
O21 J:TDP611 4.5 61.3 1.0
CA J:GLY432 4.6 65.9 1.0
C J:GLY432 4.7 66.6 1.0
N J:SER461 4.8 80.0 1.0
CA J:ASN460 4.8 79.2 1.0
C J:ASN460 4.8 80.3 1.0
C J:ASP433 4.9 66.7 1.0
C J:LEU463 4.9 73.3 0.5

Reference:

P.Neumann, A.Weidner, A.Pech, M.T.Stubbs, K.Tittmann. Structural Basis For Membrane Binding and Catalytic Activation of the Peripheral Membrane Enzyme Pyruvate Oxidase From Escherichia Coli. Proc.Natl.Acad.Sci.Usa V. 105 17390 2008.
ISSN: ISSN 0027-8424
PubMed: 18988747
DOI: 10.1073/PNAS.0805027105
Page generated: Sun Aug 10 20:43:11 2025

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