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Magnesium in PDB 2whi: Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.:
6.3.1.2;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate., PDB code: 2whi was solved by M.T.Nilsson, W.W.Krajewski, T.A.Jones, S.L.Mowbray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.81 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 133.210, 228.760, 202.700, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 23.1

Other elements in 2whi:

The structure of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. also contains other interesting chemical elements:

Chlorine (Cl) 18 atoms

Magnesium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 18;

Binding sites:

The binding sites of Magnesium atom in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. (pdb code 2whi). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 18 binding sites of Magnesium where determined in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate., PDB code: 2whi:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 18 in 2whi

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Magnesium binding site 1 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:25.7
occ:1.00
OE2 A:GLU227 1.9 22.4 1.0
OE2 A:GLU135 2.1 21.1 1.0
OE2 A:GLU219 2.1 21.0 1.0
O A:HOH2159 2.2 19.5 1.0
O2A A:P3S505 2.3 25.1 1.0
NE A:P3S505 2.5 24.9 1.0
PA A:P3S505 3.0 25.3 1.0
CD A:GLU219 3.0 20.8 1.0
CD A:GLU227 3.1 22.7 1.0
CD A:GLU135 3.1 20.9 1.0
SD A:P3S505 3.5 24.4 1.0
CG A:GLU135 3.6 20.6 1.0
OE1 A:GLU227 3.7 24.3 1.0
CG A:GLU219 3.8 20.7 1.0
OE1 A:GLU219 3.9 20.5 1.0
MG A:MG504 3.9 25.2 1.0
CE A:P3S505 3.9 24.3 1.0
CG A:P3S505 3.9 24.7 1.0
O3A A:P3S505 4.1 25.7 1.0
O1A A:P3S505 4.1 24.3 1.0
OE1 A:GLU135 4.2 21.4 1.0
OE2 A:GLU133 4.3 26.4 1.0
CB A:P3S505 4.3 24.6 1.0
CG A:GLU227 4.3 21.9 1.0
O A:HOH2070 4.5 19.2 1.0
O A:HOH2156 4.5 26.9 1.0
CB A:GLU227 4.5 21.7 1.0
CE1 A:HIS217 4.6 19.7 1.0
CE1 A:HIS276 4.7 22.8 1.0
OE A:P3S505 4.8 25.2 1.0
N A:P3S505 5.0 24.6 1.0

Magnesium binding site 2 out of 18 in 2whi

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Magnesium binding site 2 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg503

b:27.3
occ:1.00
O2 A:PO4506 2.0 37.9 1.0
OE2 A:GLU366 2.0 24.1 1.0
O3A A:P3S505 2.0 25.7 1.0
OE1 A:GLU133 2.3 25.7 1.0
ND1 A:HIS276 2.4 22.1 1.0
OE2 A:GLU133 2.4 26.4 1.0
CD A:GLU133 2.7 25.7 1.0
P A:PO4506 3.2 38.6 1.0
CE1 A:HIS276 3.2 22.8 1.0
CD A:GLU366 3.3 24.8 1.0
PA A:P3S505 3.4 25.3 1.0
CG A:HIS276 3.4 23.0 1.0
O3 A:PO4506 3.4 37.3 1.0
CB A:HIS276 3.7 23.2 1.0
O2A A:P3S505 3.7 25.1 1.0
NH1 A:ARG368 3.7 24.7 1.0
O A:HOH2159 3.8 19.5 1.0
MG A:MG504 3.9 25.2 1.0
OE1 A:GLU366 4.0 25.1 1.0
NH1 A:ARG352 4.1 25.8 1.0
NE2 A:HIS278 4.1 26.7 1.0
O4 A:PO4506 4.1 39.4 1.0
CG A:GLU133 4.2 24.3 1.0
O1 A:PO4506 4.3 39.5 1.0
NE A:P3S505 4.3 24.9 1.0
CG A:GLU366 4.3 24.9 1.0
NE2 A:HIS276 4.4 22.7 1.0
O1A A:P3S505 4.4 24.3 1.0
CD2 A:HIS276 4.5 22.9 1.0
CB A:GLU133 4.8 23.9 1.0
CZ A:ARG368 4.8 24.8 1.0
O A:HOH2161 4.8 22.4 1.0
CE1 A:HIS278 4.9 26.7 1.0

Magnesium binding site 3 out of 18 in 2whi

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Magnesium binding site 3 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg504

b:25.2
occ:1.00
O3 A:PO4506 2.1 37.3 1.0
O A:HOH2161 2.1 22.4 1.0
O2A A:P3S505 2.1 25.1 1.0
OE2 A:GLU133 2.2 26.4 1.0
O A:HOH2156 2.3 26.9 1.0
OE1 A:GLU227 2.3 24.3 1.0
CD A:GLU227 3.2 22.7 1.0
CD A:GLU133 3.2 25.7 1.0
P A:PO4506 3.3 38.6 1.0
PA A:P3S505 3.3 25.3 1.0
OE2 A:GLU227 3.5 22.4 1.0
O A:HOH2159 3.5 19.5 1.0
O4 A:PO4506 3.6 39.4 1.0
O3A A:P3S505 3.7 25.7 1.0
O2 A:PO4506 3.8 37.9 1.0
MG A:MG503 3.9 27.3 1.0
MG A:MG502 3.9 25.7 1.0
OD1 A:ASN229 3.9 26.4 1.0
CG A:GLU133 4.0 24.3 1.0
O A:HOH2125 4.1 24.0 1.0
O1A A:P3S505 4.1 24.3 1.0
OE1 A:GLU133 4.1 25.7 1.0
NZ A:LYS215 4.3 29.5 1.0
ND2 A:ASN229 4.4 24.2 1.0
CB A:GLU133 4.4 23.9 1.0
O1 A:PO4506 4.5 39.5 1.0
NE A:P3S505 4.6 24.9 1.0
NE2 A:HIS217 4.6 19.6 1.0
CG A:ASN229 4.6 24.9 1.0
CG A:GLU227 4.6 21.9 1.0
O A:HOH2275 4.7 22.9 1.0

Magnesium binding site 4 out of 18 in 2whi

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Magnesium binding site 4 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg502

b:25.7
occ:1.00
OE2 B:GLU227 2.0 22.3 1.0
O B:HOH2274 2.1 19.7 1.0
OE2 B:GLU135 2.2 21.0 1.0
O2A B:P3S505 2.2 24.9 1.0
OE2 B:GLU219 2.2 21.1 1.0
NE B:P3S505 2.4 25.0 1.0
PA B:P3S505 2.9 25.0 1.0
CD B:GLU219 3.1 20.9 1.0
CD B:GLU227 3.1 22.8 1.0
CD B:GLU135 3.2 20.7 1.0
SD B:P3S505 3.5 24.6 1.0
OE1 B:GLU227 3.6 24.2 1.0
MG B:MG504 3.7 25.1 1.0
CG B:GLU135 3.8 20.5 1.0
CE B:P3S505 3.9 24.3 1.0
OE1 B:GLU219 3.9 20.7 1.0
CG B:GLU219 3.9 20.7 1.0
O3A B:P3S505 3.9 25.5 1.0
CG B:P3S505 4.0 24.8 1.0
O1A B:P3S505 4.0 24.1 1.0
OE2 B:GLU133 4.2 26.4 1.0
OE1 B:GLU135 4.2 21.5 1.0
CB B:P3S505 4.3 24.7 1.0
CG B:GLU227 4.4 21.9 1.0
O B:HOH2071 4.5 19.1 1.0
O B:HOH2155 4.5 26.9 1.0
CE1 B:HIS276 4.6 22.8 1.0
CB B:GLU227 4.6 21.6 1.0
CE1 B:HIS217 4.6 19.7 1.0
OE B:P3S505 4.7 25.0 1.0
ND1 B:HIS276 4.9 22.4 1.0
MG B:MG503 5.0 27.2 1.0

Magnesium binding site 5 out of 18 in 2whi

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Magnesium binding site 5 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg503

b:27.2
occ:1.00
O3A B:P3S505 2.0 25.5 1.0
O2 B:PO4506 2.0 37.7 1.0
OE2 B:GLU366 2.1 23.9 1.0
OE1 B:GLU133 2.3 25.6 1.0
OE2 B:GLU133 2.4 26.4 1.0
ND1 B:HIS276 2.4 22.4 1.0
CD B:GLU133 2.6 25.6 1.0
P B:PO4506 3.2 38.9 1.0
CE1 B:HIS276 3.2 22.8 1.0
PA B:P3S505 3.3 25.0 1.0
CD B:GLU366 3.4 24.7 1.0
O3 B:PO4506 3.4 37.4 1.0
CG B:HIS276 3.4 22.9 1.0
O2A B:P3S505 3.6 24.9 1.0
O B:HOH2274 3.7 19.7 1.0
CB B:HIS276 3.8 23.2 1.0
MG B:MG504 3.8 25.1 1.0
NH1 B:ARG368 3.8 24.6 1.0
OE1 B:GLU366 4.1 25.0 1.0
CG B:GLU133 4.1 24.3 1.0
NH1 B:ARG352 4.1 25.7 1.0
O4 B:PO4506 4.1 39.5 1.0
NE2 B:HIS278 4.1 26.8 1.0
NE B:P3S505 4.3 25.0 1.0
O1 B:PO4506 4.3 39.3 1.0
O1A B:P3S505 4.3 24.1 1.0
NE2 B:HIS276 4.4 22.6 1.0
CG B:GLU366 4.4 24.9 1.0
CD2 B:HIS276 4.5 22.8 1.0
CB B:GLU133 4.7 23.8 1.0
O B:HOH2160 4.8 22.3 1.0
CZ B:ARG368 4.8 24.9 1.0
MG B:MG502 5.0 25.7 1.0
CE1 B:HIS278 5.0 26.6 1.0

Magnesium binding site 6 out of 18 in 2whi

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Magnesium binding site 6 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg504

b:25.1
occ:1.00
O3 B:PO4506 2.1 37.4 1.0
O2A B:P3S505 2.1 24.9 1.0
O B:HOH2160 2.2 22.3 1.0
OE2 B:GLU133 2.2 26.4 1.0
O B:HOH2155 2.3 26.9 1.0
OE1 B:GLU227 2.3 24.2 1.0
CD B:GLU227 3.2 22.8 1.0
CD B:GLU133 3.3 25.6 1.0
PA B:P3S505 3.3 25.0 1.0
P B:PO4506 3.3 38.9 1.0
OE2 B:GLU227 3.4 22.3 1.0
O B:HOH2274 3.6 19.7 1.0
O4 B:PO4506 3.7 39.5 1.0
MG B:MG502 3.7 25.7 1.0
O3A B:P3S505 3.7 25.5 1.0
MG B:MG503 3.8 27.2 1.0
O2 B:PO4506 3.9 37.7 1.0
OD1 B:ASN229 4.0 26.4 1.0
CG B:GLU133 4.0 24.3 1.0
O B:HOH2123 4.0 24.1 1.0
O1A B:P3S505 4.1 24.1 1.0
OE1 B:GLU133 4.2 25.6 1.0
NZ B:LYS215 4.3 29.4 1.0
ND2 B:ASN229 4.4 24.1 1.0
CB B:GLU133 4.4 23.8 1.0
NE B:P3S505 4.5 25.0 1.0
O1 B:PO4506 4.5 39.3 1.0
NE2 B:HIS217 4.5 19.7 1.0
O B:HOH2276 4.6 22.5 1.0
CG B:GLU227 4.6 21.9 1.0
CG B:ASN229 4.6 24.8 1.0

Magnesium binding site 7 out of 18 in 2whi

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Magnesium binding site 7 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg502

b:25.5
occ:1.00
OE2 C:GLU227 2.0 22.5 1.0
OE2 C:GLU219 2.1 20.7 1.0
OE2 C:GLU135 2.2 21.0 1.0
O C:HOH2157 2.2 19.8 1.0
O2A C:P3S505 2.2 25.1 1.0
NE C:P3S505 2.4 24.9 1.0
PA C:P3S505 2.9 25.7 1.0
CD C:GLU219 3.1 20.9 1.0
CD C:GLU227 3.2 22.9 1.0
CD C:GLU135 3.2 20.9 1.0
SD C:P3S505 3.5 24.6 1.0
OE1 C:GLU227 3.7 24.3 1.0
CG C:GLU135 3.8 20.6 1.0
MG C:MG504 3.8 25.0 1.0
OE1 C:GLU219 3.9 20.8 1.0
CG C:GLU219 3.9 20.7 1.0
CE C:P3S505 3.9 24.2 1.0
CG C:P3S505 3.9 24.8 1.0
O3A C:P3S505 3.9 25.6 1.0
O1A C:P3S505 4.0 24.3 1.0
CB C:P3S505 4.2 24.6 1.0
OE2 C:GLU133 4.2 26.3 1.0
OE1 C:GLU135 4.3 21.4 1.0
CG C:GLU227 4.4 21.8 1.0
O C:HOH2154 4.4 26.9 1.0
O C:HOH2069 4.4 19.3 1.0
CE1 C:HIS276 4.6 22.7 1.0
CE1 C:HIS217 4.6 19.8 1.0
CB C:GLU227 4.6 21.7 1.0
OE C:P3S505 4.7 25.1 1.0
ND1 C:HIS276 4.9 22.3 1.0

Magnesium binding site 8 out of 18 in 2whi

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Magnesium binding site 8 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg503

b:27.3
occ:1.00
O3A C:P3S505 1.9 25.6 1.0
O2 C:PO4506 2.0 37.8 1.0
OE2 C:GLU366 2.1 24.1 1.0
ND1 C:HIS276 2.4 22.3 1.0
OE2 C:GLU133 2.4 26.3 1.0
OE1 C:GLU133 2.4 25.6 1.0
CD C:GLU133 2.8 25.6 1.0
P C:PO4506 3.2 38.6 1.0
CE1 C:HIS276 3.2 22.7 1.0
PA C:P3S505 3.2 25.7 1.0
CD C:GLU366 3.3 24.7 1.0
O3 C:PO4506 3.3 37.4 1.0
CG C:HIS276 3.5 23.0 1.0
O2A C:P3S505 3.6 25.1 1.0
NH1 C:ARG368 3.7 24.7 1.0
O C:HOH2157 3.8 19.8 1.0
CB C:HIS276 3.8 23.2 1.0
MG C:MG504 3.8 25.0 1.0
OE1 C:GLU366 4.0 25.2 1.0
NH1 C:ARG352 4.0 25.7 1.0
O4 C:PO4506 4.1 39.3 1.0
NE C:P3S505 4.2 24.9 1.0
NE2 C:HIS278 4.2 26.7 1.0
O1 C:PO4506 4.2 39.5 1.0
CG C:GLU133 4.2 24.3 1.0
O1A C:P3S505 4.3 24.3 1.0
NE2 C:HIS276 4.4 22.8 1.0
CG C:GLU366 4.4 24.9 1.0
CD2 C:HIS276 4.5 22.9 1.0
CZ C:ARG368 4.7 24.9 1.0
CB C:GLU133 4.9 23.8 1.0
O C:HOH2159 4.9 22.5 1.0

Magnesium binding site 9 out of 18 in 2whi

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Magnesium binding site 9 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg504

b:25.0
occ:1.00
O2A C:P3S505 2.1 25.1 1.0
O3 C:PO4506 2.1 37.4 1.0
O C:HOH2159 2.1 22.5 1.0
OE2 C:GLU133 2.2 26.3 1.0
O C:HOH2154 2.2 26.9 1.0
OE1 C:GLU227 2.3 24.3 1.0
CD C:GLU227 3.2 22.9 1.0
CD C:GLU133 3.3 25.6 1.0
PA C:P3S505 3.3 25.7 1.0
P C:PO4506 3.3 38.6 1.0
OE2 C:GLU227 3.4 22.5 1.0
O C:HOH2157 3.5 19.8 1.0
O3A C:P3S505 3.7 25.6 1.0
O4 C:PO4506 3.7 39.3 1.0
MG C:MG502 3.8 25.5 1.0
MG C:MG503 3.8 27.3 1.0
O2 C:PO4506 3.9 37.8 1.0
OD1 C:ASN229 3.9 26.3 1.0
CG C:GLU133 3.9 24.3 1.0
O C:HOH2121 4.0 24.2 1.0
O1A C:P3S505 4.1 24.3 1.0
OE1 C:GLU133 4.2 25.6 1.0
NZ C:LYS215 4.3 29.4 1.0
ND2 C:ASN229 4.3 24.3 1.0
CB C:GLU133 4.4 23.8 1.0
NE2 C:HIS217 4.5 19.6 1.0
O1 C:PO4506 4.5 39.5 1.0
NE C:P3S505 4.6 24.9 1.0
CG C:ASN229 4.6 24.9 1.0
CG C:GLU227 4.6 21.8 1.0
O C:HOH2272 4.8 23.0 1.0

Magnesium binding site 10 out of 18 in 2whi

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Magnesium binding site 10 out of 18 in the Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Crystal Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with A Purine Analogue Inhibitor and L-Methionine-S- Sulfoximine Phosphate. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg502

b:25.3
occ:1.00
OE2 D:GLU227 2.0 22.5 1.0
OE2 D:GLU135 2.1 21.1 1.0
O D:HOH2275 2.1 19.5 1.0
OE2 D:GLU219 2.2 20.8 1.0
O2A D:P3S505 2.3 25.0 1.0
NE D:P3S505 2.4 24.9 1.0
PA D:P3S505 3.0 25.1 1.0
CD D:GLU219 3.1 20.7 1.0
CD D:GLU227 3.1 22.8 1.0
CD D:GLU135 3.1 20.9 1.0
SD D:P3S505 3.5 24.4 1.0
CG D:GLU135 3.6 20.7 1.0
OE1 D:GLU227 3.7 24.2 1.0
MG D:MG504 3.8 25.1 1.0
CG D:GLU219 3.8 20.8 1.0
OE1 D:GLU219 3.9 20.5 1.0
CE D:P3S505 3.9 24.2 1.0
CG D:P3S505 3.9 24.7 1.0
O3A D:P3S505 4.0 25.5 1.0
O1A D:P3S505 4.1 24.2 1.0
OE1 D:GLU135 4.2 21.3 1.0
OE2 D:GLU133 4.2 26.2 1.0
CB D:P3S505 4.2 24.6 1.0
CG D:GLU227 4.3 21.9 1.0
O D:HOH2071 4.3 19.4 1.0
O D:HOH2154 4.5 26.9 1.0
CB D:GLU227 4.5 21.7 1.0
CE1 D:HIS276 4.6 22.7 1.0
CE1 D:HIS217 4.6 19.6 1.0
OE D:P3S505 4.8 25.1 1.0
ND1 D:HIS276 4.9 22.1 1.0

Reference:

M.T.Nilsson, W.W.Krajewski, S.Yellagunda, S.Prabhumurthy, G.N.Chamarahally, C.Siddamadappa, B.R.Srinivasa, S.Yahiaoui, M.Larhed, A.Karlen, T.A.Jones, S.L.Mowbray. Structural Basis For the Inhibition of Mycobacterium Tuberculosis Glutamine Synthetase By Novel Atp-Competitive Inhibitors. J.Mol.Biol. V. 393 504 2009.
ISSN: ISSN 0022-2836
PubMed: 19695264
DOI: 10.1016/J.JMB.2009.08.028
Page generated: Wed Aug 14 06:06:32 2024

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