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Magnesium in PDB 9otp: Human Glutamine Synthetase R298A Decamer Under Turnover Conditions

Enzymatic activity of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions

All present enzymatic activity of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions:
2.3.1.225; 6.3.1.2;

Magnesium Binding Sites:

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

Binding sites:

The binding sites of Magnesium atom in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions (pdb code 9otp). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 20 binding sites of Magnesium where determined in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions, PDB code: 9otp:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Magnesium binding site 1 out of 20 in 9otp

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Magnesium binding site 1 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1001

b:95.9
occ:1.00
O2B A:ADP1000 1.8 97.1 1.0
OE2 A:GLU338 1.9 111.0 1.0
HD2 A:HIS253 2.4 95.6 1.0
OE2 A:GLU134 2.6 86.4 1.0
PB A:ADP1000 2.8 106.9 1.0
CD A:GLU338 2.9 111.4 1.0
OE1 A:GLU134 2.9 87.7 1.0
O3A A:ADP1000 3.0 106.6 1.0
CD A:GLU134 3.1 83.4 1.0
CD2 A:HIS253 3.2 95.4 1.0
O3B A:ADP1000 3.3 101.2 1.0
OE1 A:GLU338 3.3 115.0 1.0
HB2 A:HIS253 3.6 96.8 1.0
HH12 A:ARG340 3.6 108.9 1.0
HH11 A:ARG340 3.9 108.7 1.0
CG A:HIS253 3.9 98.9 1.0
MG A:MG1002 3.9 72.2 1.0
NH1 A:ARG340 4.0 109.3 1.0
HB3 A:HIS253 4.1 97.5 1.0
CB A:HIS253 4.1 98.9 1.0
O1B A:ADP1000 4.2 95.8 1.0
HH12 A:ARG319 4.2 114.7 1.0
CG A:GLU338 4.2 108.8 1.0
HG3 A:GLU338 4.3 107.7 1.0
NE2 A:HIS253 4.3 99.7 1.0
HE2 A:HIS253 4.4 97.0 1.0
PA A:ADP1000 4.5 110.7 1.0
CG A:GLU134 4.6 74.7 1.0
HH11 A:ARG319 4.6 115.1 1.0
NH1 A:ARG319 4.7 115.6 1.0
HG2 A:GLU338 4.7 108.0 1.0
HG2 A:ARG340 4.8 108.5 1.0
HG3 A:GLU134 4.8 76.6 1.0
HD22 A:ASN255 4.8 93.5 1.0
O2A A:ADP1000 4.9 93.8 1.0
HH11 A:ARG324 4.9 112.5 1.0

Magnesium binding site 2 out of 20 in 9otp

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Magnesium binding site 2 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1002

b:72.2
occ:1.00
O3B A:ADP1000 2.0 101.2 1.0
OE1 A:GLU134 2.2 87.7 1.0
O2A A:ADP1000 2.3 93.8 1.0
OE2 A:GLU203 2.6 74.0 1.0
PB A:ADP1000 3.1 106.9 1.0
CD A:GLU134 3.1 83.4 1.0
O3A A:ADP1000 3.1 106.6 1.0
PA A:ADP1000 3.3 110.7 1.0
HE21 A:GLN205 3.6 63.1 1.0
CD A:GLU203 3.6 71.9 1.0
OE2 A:GLU134 3.8 86.4 1.0
HB3 A:GLU134 3.9 76.6 1.0
OE1 A:GLU203 3.9 73.7 1.0
HG2 A:GLU134 3.9 77.7 1.0
MG A:MG1001 3.9 95.9 1.0
CG A:GLU134 4.0 74.7 1.0
O2B A:ADP1000 4.0 97.1 1.0
NE2 A:GLN205 4.1 65.9 1.0
O1B A:ADP1000 4.2 95.8 1.0
HG2 A:GLN205 4.3 61.9 1.0
O5' A:ADP1000 4.3 99.6 1.0
O1A A:ADP1000 4.4 99.4 1.0
HE22 A:GLN205 4.4 61.8 1.0
CB A:GLU134 4.4 68.6 1.0
HG3 A:GLN205 4.5 62.3 1.0
HD2 A:HIS253 4.6 95.6 1.0
OD1 A:ASN194 4.6 62.2 1.0
HB2 A:GLU134 4.6 76.4 1.0
CD A:GLN205 4.7 68.2 1.0
CG A:GLN205 4.7 56.1 1.0
HG3 A:GLU134 4.9 76.6 1.0
CG A:GLU203 4.9 62.4 1.0
HG2 A:GLU203 4.9 60.5 1.0

Magnesium binding site 3 out of 20 in 9otp

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Magnesium binding site 3 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg402

b:87.6
occ:1.00
O2B B:ADP401 1.8 95.3 1.0
OE2 B:GLU338 1.9 109.4 1.0
HD1 B:HIS253 2.1 94.4 1.0
OE2 B:GLU134 2.5 83.9 1.0
PB B:ADP401 2.9 101.4 1.0
CD B:GLU338 2.9 108.0 1.0
OE1 B:GLU134 2.9 87.4 1.0
ND1 B:HIS253 2.9 92.6 1.0
CD B:GLU134 3.1 81.5 1.0
O3A B:ADP401 3.1 102.9 1.0
OE1 B:GLU338 3.3 109.9 1.0
O3B B:ADP401 3.3 94.1 1.0
HB2 B:HIS253 3.6 95.8 1.0
HH21 B:ARG340 3.8 107.7 1.0
CE1 B:HIS253 3.8 95.6 1.0
MG B:MG403 3.8 68.7 1.0
CG B:HIS253 3.9 97.9 1.0
HE1 B:HIS253 3.9 95.4 1.0
HB3 B:HIS253 3.9 96.1 1.0
CB B:HIS253 4.0 99.9 1.0
NH2 B:ARG340 4.1 111.8 1.0
HH22 B:ARG340 4.2 107.7 1.0
O1B B:ADP401 4.2 93.7 1.0
CG B:GLU338 4.3 104.7 1.0
HG3 B:GLU338 4.3 104.7 1.0
HH11 B:ARG324 4.5 111.5 1.0
CG B:GLU134 4.6 71.5 1.0
HH12 B:ARG324 4.6 111.4 1.0
HH12 B:ARG319 4.6 115.4 1.0
HH11 B:ARG319 4.7 115.4 1.0
PA B:ADP401 4.7 103.0 1.0
HG2 B:GLU338 4.7 104.8 1.0
NH1 B:ARG324 4.7 111.7 1.0
CZ B:ARG340 4.7 108.5 1.0
H5'2 B:ADP401 4.8 91.8 1.0
HG3 B:GLU134 4.8 74.0 1.0
HE B:ARG340 4.8 107.5 1.0
HD22 B:ASN255 4.8 91.2 1.0
NE2 B:HIS253 5.0 95.6 1.0
NH1 B:ARG319 5.0 116.2 1.0

Magnesium binding site 4 out of 20 in 9otp

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Magnesium binding site 4 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg403

b:68.7
occ:1.00
OE1 B:GLU134 2.1 87.4 1.0
O1A B:ADP401 2.4 92.4 1.0
O3B B:ADP401 2.6 94.1 1.0
OE2 B:GLU203 2.6 71.8 1.0
O3A B:ADP401 2.8 102.9 1.0
CD B:GLU134 3.1 81.5 1.0
PA B:ADP401 3.2 103.0 1.0
PB B:ADP401 3.3 101.4 1.0
CD B:GLU203 3.6 72.5 1.0
HE21 B:GLN205 3.7 63.0 1.0
OE2 B:GLU134 3.8 83.9 1.0
OE1 B:GLU203 3.8 76.5 1.0
HB3 B:GLU134 3.8 74.3 1.0
MG B:MG402 3.8 87.6 1.0
HG2 B:GLU134 3.9 74.9 1.0
CG B:GLU134 4.0 71.5 1.0
O2B B:ADP401 4.1 95.3 1.0
O2A B:ADP401 4.1 93.4 1.0
NE2 B:GLN205 4.1 67.3 1.0
HG2 B:GLN205 4.3 61.5 1.0
CB B:GLU134 4.4 64.6 1.0
O5' B:ADP401 4.4 94.7 1.0
HE22 B:GLN205 4.4 61.7 1.0
O1B B:ADP401 4.5 93.7 1.0
HG3 B:GLN205 4.5 62.4 1.0
HB2 B:GLU134 4.6 73.5 1.0
OD1 B:ASN194 4.6 62.0 1.0
CD B:GLN205 4.7 68.5 1.0
CG B:GLN205 4.7 58.1 1.0
HG3 B:GLU134 4.8 74.0 1.0
HD1 B:HIS253 4.9 94.4 1.0
CG B:GLU203 5.0 57.5 1.0

Magnesium binding site 5 out of 20 in 9otp

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Magnesium binding site 5 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg402

b:91.6
occ:1.00
O1B C:ADP401 1.9 97.1 1.0
OE2 C:GLU338 2.0 104.3 1.0
OE2 C:GLU134 2.2 83.3 1.0
PB C:ADP401 2.5 107.3 1.0
O2B C:ADP401 2.6 94.4 1.0
HD2 C:HIS253 2.6 92.3 1.0
O3A C:ADP401 2.9 105.8 1.0
CD C:GLU338 3.0 105.8 1.0
CD C:GLU134 3.2 79.9 1.0
OE1 C:GLU338 3.4 109.0 1.0
OE1 C:GLU134 3.5 84.0 1.0
CD2 C:HIS253 3.5 94.2 1.0
HB2 C:HIS253 3.8 93.4 1.0
MG C:MG403 3.9 67.6 1.0
HH21 C:ARG340 3.9 107.5 1.0
O3B C:ADP401 4.0 95.6 1.0
HH12 C:ARG319 4.2 113.2 1.0
CG C:HIS253 4.3 96.3 1.0
CG C:GLU338 4.3 104.1 1.0
HG3 C:GLU338 4.3 103.2 1.0
HB3 C:HIS253 4.4 93.6 1.0
CB C:HIS253 4.4 96.1 1.0
PA C:ADP401 4.4 105.7 1.0
HH11 C:ARG324 4.4 109.5 1.0
NH2 C:ARG340 4.5 108.9 1.0
HH12 C:ARG324 4.5 109.7 1.0
CG C:GLU134 4.6 72.4 1.0
NE2 C:HIS253 4.6 97.0 1.0
O5' C:ADP401 4.6 97.6 1.0
NH1 C:ARG324 4.7 109.2 1.0
HE2 C:HIS253 4.8 93.5 1.0
HH22 C:ARG340 4.8 107.7 1.0
HG2 C:GLU134 4.8 74.1 1.0
NH1 C:ARG319 4.8 112.2 1.0
HG3 C:GLU134 4.8 73.9 1.0
HG2 C:GLU338 4.8 103.2 1.0
O1A C:ADP401 4.9 100.3 1.0
HE C:ARG340 4.9 107.3 1.0
HD22 C:ASN255 5.0 91.9 1.0

Magnesium binding site 6 out of 20 in 9otp

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Magnesium binding site 6 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg403

b:67.6
occ:1.00
OE1 C:GLU134 2.3 84.0 1.0
O3A C:ADP401 2.4 105.8 1.0
OE2 C:GLU203 2.5 72.7 1.0
O2B C:ADP401 2.6 94.4 1.0
CD C:GLU134 3.1 79.9 1.0
PB C:ADP401 3.1 107.3 1.0
O2A C:ADP401 3.2 91.6 1.0
PA C:ADP401 3.4 105.7 1.0
OE2 C:GLU134 3.5 83.3 1.0
HE21 C:GLN205 3.6 61.4 1.0
CD C:GLU203 3.6 73.4 1.0
MG C:MG402 3.9 91.6 1.0
O3B C:ADP401 3.9 95.6 1.0
OE1 C:GLU203 4.0 73.1 1.0
NE2 C:GLN205 4.0 62.8 1.0
HB2 C:GLU134 4.0 73.8 1.0
HB3 C:GLU134 4.2 74.5 1.0
HG2 C:GLN205 4.2 60.7 1.0
CG C:GLU134 4.2 72.4 1.0
O1B C:ADP401 4.2 97.1 1.0
O5' C:ADP401 4.3 97.6 1.0
HE22 C:GLN205 4.3 60.8 1.0
CB C:GLU134 4.4 67.5 1.0
HG3 C:GLU134 4.4 73.9 1.0
HG3 C:GLN205 4.5 61.7 1.0
O1A C:ADP401 4.5 100.3 1.0
OD1 C:ASN194 4.6 61.5 1.0
CD C:GLN205 4.6 66.7 1.0
CG C:GLN205 4.6 56.9 1.0
HD2 C:HIS253 4.8 92.3 1.0
HG2 C:GLU203 4.8 59.4 1.0
CG C:GLU203 4.9 62.1 1.0
HG2 C:GLU134 5.0 74.1 1.0

Magnesium binding site 7 out of 20 in 9otp

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Magnesium binding site 7 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg402

b:89.3
occ:1.00
O1B D:ADP401 1.9 96.0 1.0
OE2 D:GLU338 1.9 106.5 1.0
O2B D:ADP401 2.6 96.1 1.0
OE2 D:GLU134 2.6 85.6 1.0
PB D:ADP401 2.6 111.1 1.0
CD D:GLU338 3.0 108.5 1.0
OE1 D:GLU134 3.0 90.4 1.0
CD D:GLU134 3.2 84.2 1.0
OE1 D:GLU338 3.3 111.7 1.0
O3A D:ADP401 3.4 106.1 1.0
HH21 D:ARG340 3.4 108.2 1.0
ND1 D:HIS253 3.5 98.8 1.0
HB2 D:HIS253 3.9 98.3 1.0
MG D:MG403 3.9 71.5 1.0
O3B D:ADP401 4.0 96.1 1.0
HH12 D:ARG319 4.1 112.3 1.0
HB3 D:HIS253 4.2 98.8 1.0
NH2 D:ARG340 4.2 108.2 1.0
CG D:GLU338 4.3 105.5 1.0
HG3 D:GLU338 4.3 104.8 1.0
CB D:HIS253 4.3 99.7 1.0
CG D:HIS253 4.3 101.8 1.0
HE D:ARG340 4.4 108.3 1.0
HH11 D:ARG324 4.4 110.0 1.0
CE1 D:HIS253 4.4 102.0 1.0
HE1 D:HIS253 4.5 99.0 1.0
HH12 D:ARG324 4.5 110.0 1.0
HD22 D:ASN255 4.5 93.7 1.0
HH22 D:ARG340 4.6 108.0 1.0
CG D:GLU134 4.6 76.3 1.0
NH1 D:ARG324 4.6 109.4 1.0
PA D:ADP401 4.7 107.2 1.0
NH1 D:ARG319 4.7 113.2 1.0
HG2 D:GLU338 4.8 104.9 1.0
O1A D:ADP401 4.9 102.4 1.0
HG3 D:GLU134 4.9 76.6 1.0
HH11 D:ARG319 4.9 112.4 1.0
O5' D:ADP401 4.9 97.5 1.0

Magnesium binding site 8 out of 20 in 9otp

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Magnesium binding site 8 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 8 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg403

b:71.5
occ:1.00
OE1 D:GLU134 2.1 90.4 1.0
O3A D:ADP401 2.3 106.1 1.0
O2B D:ADP401 2.3 96.1 1.0
OE2 D:GLU203 2.8 79.4 1.0
PB D:ADP401 2.9 111.1 1.0
CD D:GLU134 3.1 84.2 1.0
CD D:GLU203 3.6 75.5 1.0
OE1 D:GLU203 3.6 71.4 1.0
PA D:ADP401 3.6 107.2 1.0
OE2 D:GLU134 3.7 85.6 1.0
HE21 D:GLN205 3.8 63.2 1.0
O2A D:ADP401 3.8 94.9 1.0
HB3 D:GLU134 3.8 76.5 1.0
O3B D:ADP401 3.8 96.1 1.0
MG D:MG402 3.9 89.3 1.0
HG2 D:GLU134 3.9 77.3 1.0
O1B D:ADP401 3.9 96.0 1.0
CG D:GLU134 4.0 76.3 1.0
NE2 D:GLN205 4.2 65.0 1.0
HG2 D:GLN205 4.3 61.8 1.0
CB D:GLU134 4.3 68.9 1.0
O5' D:ADP401 4.4 97.5 1.0
HE22 D:GLN205 4.5 61.5 1.0
HG3 D:GLN205 4.5 62.5 1.0
HB2 D:GLU134 4.6 75.7 1.0
OD1 D:ASN194 4.6 61.8 1.0
O1A D:ADP401 4.7 102.4 1.0
CD D:GLN205 4.7 68.4 1.0
CG D:GLN205 4.7 57.5 1.0
HG3 D:GLU134 4.8 76.6 1.0

Magnesium binding site 9 out of 20 in 9otp

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Magnesium binding site 9 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 9 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg402

b:90.3
occ:1.00
O2B E:ADP401 1.8 97.7 1.0
OE2 E:GLU338 1.9 108.0 1.0
HD2 E:HIS253 2.4 95.4 1.0
OE2 E:GLU134 2.5 84.9 1.0
OE1 E:GLU134 2.8 86.2 1.0
PB E:ADP401 2.9 109.0 1.0
CD E:GLU338 2.9 108.5 1.0
CD E:GLU134 3.0 82.3 1.0
O3A E:ADP401 3.1 104.5 1.0
CD2 E:HIS253 3.3 95.2 1.0
OE1 E:GLU338 3.3 112.0 1.0
O3B E:ADP401 3.4 100.3 1.0
HB2 E:HIS253 3.5 96.0 1.0
HH12 E:ARG340 3.7 108.2 1.0
HB3 E:HIS253 3.8 96.6 1.0
CG E:HIS253 3.9 98.9 1.0
CB E:HIS253 4.0 98.1 1.0
HH11 E:ARG340 4.0 108.4 1.0
MG E:MG403 4.0 72.6 1.0
NH1 E:ARG340 4.1 109.1 1.0
O1B E:ADP401 4.2 96.2 1.0
CG E:GLU338 4.2 105.6 1.0
HG3 E:GLU338 4.2 105.4 1.0
NE2 E:HIS253 4.4 98.7 1.0
HH12 E:ARG319 4.5 114.4 1.0
CG E:GLU134 4.5 74.8 1.0
PA E:ADP401 4.6 106.5 1.0
HH11 E:ARG324 4.6 113.2 1.0
HG2 E:GLU338 4.7 105.8 1.0
HG3 E:GLU134 4.7 76.5 1.0
HH12 E:ARG324 4.8 113.0 1.0
HG2 E:ARG340 4.8 108.2 1.0
HB2 E:GLU134 4.9 76.2 1.0
NH1 E:ARG324 4.9 113.8 1.0
HD22 E:ASN255 4.9 93.1 1.0
O2A E:ADP401 5.0 93.9 1.0
NH1 E:ARG319 5.0 114.7 1.0

Magnesium binding site 10 out of 20 in 9otp

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Magnesium binding site 10 out of 20 in the Human Glutamine Synthetase R298A Decamer Under Turnover Conditions


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 10 of Human Glutamine Synthetase R298A Decamer Under Turnover Conditions within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg403

b:72.6
occ:1.00
O3B E:ADP401 2.1 100.3 1.0
OE1 E:GLU134 2.3 86.2 1.0
O2A E:ADP401 2.3 93.9 1.0
OE2 E:GLU203 2.6 77.8 1.0
O3A E:ADP401 3.1 104.5 1.0
PB E:ADP401 3.2 109.0 1.0
CD E:GLU134 3.2 82.3 1.0
PA E:ADP401 3.3 106.5 1.0
CD E:GLU203 3.5 74.2 1.0
HE21 E:GLN205 3.6 63.4 1.0
OE1 E:GLU203 3.8 75.3 1.0
HB3 E:GLU134 3.8 76.5 1.0
OE2 E:GLU134 3.9 84.9 1.0
HG2 E:GLU134 3.9 77.2 1.0
NE2 E:GLN205 4.0 64.9 1.0
MG E:MG402 4.0 90.3 1.0
O2B E:ADP401 4.1 97.7 1.0
CG E:GLU134 4.1 74.8 1.0
HG2 E:GLN205 4.3 62.6 1.0
O1B E:ADP401 4.3 96.2 1.0
HE22 E:GLN205 4.4 62.6 1.0
O1A E:ADP401 4.4 96.4 1.0
O5' E:ADP401 4.4 98.7 1.0
CB E:GLU134 4.4 69.0 1.0
HG3 E:GLN205 4.5 63.2 1.0
OD1 E:ASN194 4.5 63.1 1.0
CD E:GLN205 4.6 66.9 1.0
HB2 E:GLU134 4.6 76.2 1.0
CG E:GLN205 4.7 58.6 1.0
CG E:GLU203 4.9 61.5 1.0
HG3 E:GLU134 4.9 76.5 1.0
HG2 E:GLU203 4.9 60.6 1.0
HD2 E:HIS253 5.0 95.4 1.0

Reference:

E.R.Greene, R.S.Muniz, H.Yamamura, S.Hoff, P.Bajaj, D.J.Lee, E.M.Thompson, A.Arada, M.Bonomi, J.M.Kollman, J.S.Fraser. Product-Stabilized Filamentation By Human Glutamine Synthetase Allosterically Tunes Metabolic Activity To Be Published.
Page generated: Sat Aug 16 07:06:55 2025

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