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Magnesium in PDB 4lnn: B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs

Enzymatic activity of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs

All present enzymatic activity of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs:
6.3.1.2;

Protein crystallography data

The structure of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs, PDB code: 4lnn was solved by M.A.Schumacher, N.Chinnam, N.Tonthat, S.Fisher, L.Wray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 84.25 / 3.10
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 109.990, 138.380, 138.740, 119.80, 90.19, 93.85
R / Rfree (%) 21.7 / 26.7

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 25;

Binding sites:

The binding sites of Magnesium atom in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs (pdb code 4lnn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 25 binding sites of Magnesium where determined in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs, PDB code: 4lnn:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 25 in 4lnn

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Magnesium binding site 1 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:10.9
occ:1.00
 OE1 A:GLU189 2.7 46.7 1.0
OE2 A:GLU134 2.7 51.8 1.0
OE2 A:GLU196 2.9 53.3 1.0
O A:HOH603 3.2 25.9 1.0
CD A:GLU189 3.5 47.2 1.0
CD A:GLU196 3.7 52.4 1.0
OE2 A:GLU189 3.8 46.3 1.0
CD A:GLU134 3.8 51.9 1.0
OE1 A:GLU196 3.9 53.4 1.0
CE1 A:HIS245 4.4 59.8 1.0
CG A:GLU189 4.5 47.0 1.0
CG A:GLU134 4.6 50.8 1.0
OE1 A:GLU134 4.7 53.4 1.0
NE2 A:HIS187 4.8 56.9 1.0
OH A:TYR156 4.9 49.3 1.0
ND1 A:HIS245 4.9 59.2 1.0
NE2 A:HIS245 5.0 59.9 1.0

Magnesium binding site 2 out of 25 in 4lnn

Go back to Magnesium Binding Sites List in 4lnn
Magnesium binding site 2 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:19.7
occ:1.00
 OE1 A:GLU132 2.4 48.9 1.0
OE2 A:GLU132 2.4 48.7 1.0
CD A:GLU132 2.7 49.6 1.0
OE1 A:GLU333 2.9 57.5 1.0
OE2 A:GLU333 3.3 55.9 1.0
CD A:GLU333 3.4 57.2 1.0
ND1 A:HIS245 3.7 59.2 1.0
O A:HOH603 3.8 25.9 1.0
CG A:GLU132 4.3 49.1 1.0
CE1 A:HIS245 4.4 59.8 1.0
ND2 A:ASN247 4.5 61.5 1.0
O A:HOH605 4.6 23.0 1.0
CG A:HIS245 4.7 59.6 1.0
CB A:HIS245 4.9 59.2 1.0
CG A:GLU333 4.9 57.1 1.0
OE1 B:GLU65 5.0 87.7 1.0

Magnesium binding site 3 out of 25 in 4lnn

Go back to Magnesium Binding Sites List in 4lnn
Magnesium binding site 3 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:21.4
occ:1.00
 OE1 B:GLU189 2.3 48.2 1.0
OE2 B:GLU196 2.5 42.1 1.0
OE2 B:GLU134 2.5 57.5 1.0
O B:HOH610 3.1 34.2 1.0
CD B:GLU196 3.4 43.1 1.0
CD B:GLU189 3.5 48.6 1.0
OE1 B:GLU196 3.7 41.5 1.0
CD B:GLU134 3.7 58.6 1.0
NE2 B:HIS187 4.1 52.3 1.0
OE2 B:GLU189 4.4 49.2 1.0
CE1 B:HIS187 4.4 52.0 1.0
CG B:GLU189 4.4 48.2 1.0
OE1 B:GLU134 4.5 58.9 1.0
CG B:GLU134 4.5 57.1 1.0
CE1 B:HIS245 4.6 58.4 1.0
CG B:GLU196 4.8 43.8 1.0
OE2 B:GLU132 5.0 55.6 1.0

Magnesium binding site 4 out of 25 in 4lnn

Go back to Magnesium Binding Sites List in 4lnn
Magnesium binding site 4 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg502

b:23.5
occ:1.00
 OE1 B:GLU132 2.6 57.0 1.0
OE2 B:GLU333 2.6 57.8 1.0
OE2 B:GLU132 2.7 55.6 1.0
CD B:GLU132 3.0 55.9 1.0
CD B:GLU333 3.6 57.4 1.0
OE1 B:GLU333 3.8 59.4 1.0
ND1 B:HIS245 4.4 58.0 1.0
CG B:GLU132 4.5 56.1 1.0
OE1 C:GLU65 4.9 85.6 1.0
OD1 B:ASN247 4.9 62.7 1.0

Magnesium binding site 5 out of 25 in 4lnn

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Magnesium binding site 5 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg503

b:92.7
occ:1.00
 NE2 B:HIS416 2.7 62.7 1.0
O B:VAL61 3.1 90.3 1.0
CE1 B:HIS416 3.3 61.9 1.0
CD2 B:HIS416 3.7 62.0 1.0
OE2 B:GLU58 3.8 79.7 1.0
OE1 B:GLU58 3.8 81.0 1.0
CD B:GLU58 4.0 78.6 1.0
C B:VAL61 4.3 90.2 1.0
ND1 B:HIS416 4.4 61.9 1.0
CG B:HIS416 4.6 61.2 1.0
CG1 B:ILE63 4.8 96.5 1.0
CA B:ARG62 4.9 92.1 1.0
CB B:VAL61 4.9 88.6 1.0
CD1 B:ILE63 4.9 96.9 1.0
CG2 B:VAL61 4.9 88.1 1.0
N B:ILE63 5.0 94.6 1.0

Magnesium binding site 6 out of 25 in 4lnn

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Magnesium binding site 6 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg501

b:27.3
occ:1.00
 OE1 C:GLU189 2.6 49.9 1.0
OE2 C:GLU134 2.6 53.0 1.0
OE2 C:GLU196 2.9 63.6 1.0
O C:HOH609 3.2 35.5 1.0
CD C:GLU134 3.6 53.4 1.0
CD C:GLU189 3.8 50.7 1.0
CD C:GLU196 3.8 63.9 1.0
CE1 C:HIS245 4.1 63.4 1.0
OE1 C:GLU196 4.2 66.2 1.0
OE1 C:GLU134 4.3 53.7 1.0
CG C:GLU134 4.4 51.8 1.0
OE2 C:GLU189 4.4 51.6 1.0
OE2 C:GLU132 4.5 54.0 1.0
ND1 C:HIS245 4.5 63.1 1.0
NE2 C:HIS187 4.8 50.1 1.0
NE2 C:HIS245 4.8 63.1 1.0
CG C:GLU189 4.9 50.1 1.0

Magnesium binding site 7 out of 25 in 4lnn

Go back to Magnesium Binding Sites List in 4lnn
Magnesium binding site 7 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg502

b:34.9
occ:1.00
 OE2 C:GLU333 2.5 57.4 1.0
OE1 C:GLU132 2.7 52.1 1.0
OE2 C:GLU132 2.9 54.0 1.0
CD C:GLU132 3.2 52.9 1.0
CD C:GLU333 3.4 57.4 1.0
OE1 C:GLU333 3.6 56.6 1.0
O C:HOH609 4.0 35.5 1.0
ND1 C:HIS245 4.0 63.1 1.0
NH1 C:ARG321 4.1 89.9 1.0
CG C:GLU132 4.7 51.5 1.0
CE1 C:HIS245 4.7 63.4 1.0
CZ C:ARG321 4.7 90.3 1.0
OE1 D:GLU65 4.8 97.0 1.0
CG C:GLU333 4.8 56.1 1.0

Magnesium binding site 8 out of 25 in 4lnn

Go back to Magnesium Binding Sites List in 4lnn
Magnesium binding site 8 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg502

b:8.0
occ:1.00
 OE2 D:GLU134 2.4 59.1 1.0
OE2 D:GLU196 2.5 57.1 1.0
OE1 D:GLU189 2.6 40.5 1.0
O D:HOH606 3.3 42.5 1.0
CD D:GLU196 3.5 55.9 1.0
CD D:GLU189 3.6 41.6 1.0
CD D:GLU134 3.6 59.3 1.0
OE1 D:GLU196 3.7 58.2 1.0
OE2 D:GLU189 4.2 40.2 1.0
CE1 D:HIS245 4.4 56.7 1.0
NE2 D:HIS187 4.4 58.3 1.0
OE1 D:GLU134 4.5 60.6 1.0
CG D:GLU134 4.5 58.4 1.0
CG D:GLU189 4.7 41.0 1.0
CG D:GLU196 4.9 51.5 1.0
ND1 D:HIS245 4.9 56.3 1.0
NE2 D:HIS245 5.0 55.7 1.0

Magnesium binding site 9 out of 25 in 4lnn

Go back to Magnesium Binding Sites List in 4lnn
Magnesium binding site 9 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg503

b:32.0
occ:1.00
 OE1 D:GLU132 2.5 50.3 1.0
OE1 D:GLU333 2.6 51.3 1.0
OE2 D:GLU132 2.9 50.9 1.0
CD D:GLU132 3.1 50.8 1.0
OE2 D:GLU333 3.3 50.6 1.0
CD D:GLU333 3.3 51.2 1.0
ND1 D:HIS245 3.7 56.3 1.0
OE1 E:GLU65 3.7 84.6 1.0
NH1 D:ARG321 3.9 74.8 1.0
NH1 D:ARG335 4.1 53.1 1.0
CE1 D:HIS245 4.5 56.7 1.0
CG D:GLU132 4.6 51.0 1.0
CG D:HIS245 4.7 56.1 1.0
CD E:GLU65 4.8 84.7 1.0
OD1 D:ASN247 4.8 63.3 1.0
CG D:GLU333 4.8 50.5 1.0
CB D:HIS245 4.9 56.0 1.0

Magnesium binding site 10 out of 25 in 4lnn

Go back to Magnesium Binding Sites List in 4lnn
Magnesium binding site 10 out of 25 in the B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of B. Subtilis Glutamine Synthetase Structures Reveal Large Active Site Conformational Changes and Basis For Isoenzyme Specific Regulation: Structure of Apo Form of Gs within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg501

b:22.8
occ:1.00
 OE1 E:GLU132 2.6 56.1 1.0
OE1 E:GLU333 2.6 60.8 1.0
OE2 E:GLU132 2.6 57.7 1.0
CD E:GLU132 3.0 56.7 1.0
CD E:GLU333 3.4 61.8 1.0
OE2 E:GLU333 3.4 62.6 1.0
NH1 E:ARG321 3.5 68.9 1.0
OE1 F:GLU65 3.9 88.5 1.0
ND1 E:HIS245 3.9 65.1 1.0
CG E:GLU132 4.5 54.8 1.0
CZ E:ARG321 4.6 69.2 1.0
CE1 E:HIS245 4.7 66.7 1.0
CD F:GLU65 4.8 87.3 1.0
OE2 F:GLU65 4.8 87.3 1.0
CG E:GLU333 4.8 59.4 1.0
CG E:HIS245 4.9 63.3 1.0

Reference:

D.S.Murray, N.Chinnam, N.K.Tonthat, T.Whitfill, L.V.Wray, S.H.Fisher, M.A.Schumacher. Structures of the Bacillus Subtilis Glutamine Synthetase Dodecamer Reveal Large Intersubunit Catalytic Conformational Changes Linked to A Unique Feedback Inhibition Mechanism. J.Biol.Chem. V. 288 35801 2013.
ISSN: ISSN 0021-9258
PubMed: 24158439
DOI: 10.1074/JBC.M113.519496
Page generated: Mon Aug 19 19:51:07 2024

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