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Thallium in PDB 1f1h: Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions

Enzymatic activity of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions

All present enzymatic activity of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions:
6.3.1.2;

Protein crystallography data

The structure of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions, PDB code: 1f1h was solved by H.S.Gill, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.00 / 2.67
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 231.130, 132.790, 196.780, 90.00, 102.44, 90.00
R / Rfree (%) 23.2 / 26.3

Other elements in 1f1h:

The structure of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions also contains other interesting chemical elements:

Manganese (Mn) 24 atoms

Thallium Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 24;

Binding sites:

The binding sites of Thallium atom in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions (pdb code 1f1h). This binding sites where shown within 5.0 Angstroms radius around Thallium atom.
In total 24 binding sites of Thallium where determined in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions, PDB code: 1f1h:
Jump to Thallium binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Thallium binding site 1 out of 24 in 1f1h

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Thallium binding site 1 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 1 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tl473

b:67.6
occ:0.39
 OH A:TYR179 2.9 86.1 0.4
OE2 A:GLU212 3.0 36.5 1.0
OE1 A:GLU212 3.1 40.3 1.0
OG B:SER53 3.1 55.6 0.4
CZ A:TYR179 3.2 68.5 0.4
OD1 B:ASP50 3.2 81.2 0.4
CD A:GLU212 3.4 39.6 1.0
O A:HOH1583 3.6 49.4 1.0
CE2 A:TYR179 3.7 64.9 0.4
OD2 B:ASP50 3.7 76.7 0.4
CB B:SER53 3.8 64.2 0.4
MN A:MN469 3.8 34.9 1.0
CG B:ASP50 3.9 79.0 0.4
CE1 A:TYR179 3.9 78.7 0.4
CG2 A:VAL213 4.0 28.0 1.0
O B:HOH1490 4.4 67.0 1.0
CD2 A:TYR179 4.6 52.2 0.4
OE1 A:GLU131 4.6 40.2 1.0
O B:ASP50 4.8 41.7 0.4
CD1 A:TYR179 4.8 60.5 0.4
CG A:GLU212 4.9 26.5 1.0

Thallium binding site 2 out of 24 in 1f1h

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Thallium binding site 2 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 2 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Tl474

b:75.1
occ:0.39
 OE2 A:GLU131 2.7 32.2 1.0
O A:HOH1584 2.9 48.4 1.0
OD1 A:ASN264 3.0 65.7 1.0
O A:GLY265 3.1 36.4 1.0
O A:HOH1554 3.3 53.2 1.0
CD A:GLU131 3.4 37.3 1.0
OE1 A:GLU131 3.4 40.2 1.0
CG A:ASN264 4.0 53.5 1.0
C A:GLY265 4.2 25.4 1.0
N A:GLY267 4.2 35.8 1.0
OE1 A:GLU212 4.2 40.3 1.0
NE2 A:GLN218 4.3 15.7 1.0
OE1 A:GLN218 4.3 38.9 1.0
O A:HOH1573 4.5 34.4 1.0
O A:HOH1495 4.5 24.0 1.0
CA A:SER266 4.5 26.0 1.0
CD A:GLN218 4.8 15.3 1.0
CG A:GLU131 4.8 24.8 1.0
ND2 A:ASN264 4.8 31.9 1.0
C A:SER266 4.8 33.4 1.0
CB A:ASN264 4.8 49.0 1.0
CD A:GLU212 4.8 39.6 1.0
N A:SER266 4.8 25.7 1.0
N A:GLY265 4.9 28.7 1.0

Thallium binding site 3 out of 24 in 1f1h

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Thallium binding site 3 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 3 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Tl473

b:67.6
occ:0.39
 OH B:TYR179 2.9 86.1 0.4
OE2 B:GLU212 3.0 36.5 1.0
OE1 B:GLU212 3.1 40.3 1.0
OD1 C:ASP50 3.2 81.2 0.4
CZ B:TYR179 3.2 68.5 0.4
OG C:SER53 3.3 55.6 0.4
CD B:GLU212 3.4 39.6 1.0
O B:HOH1590 3.6 49.4 1.0
CE2 B:TYR179 3.7 64.9 0.4
OD2 C:ASP50 3.7 76.7 0.4
MN B:MN469 3.8 34.9 1.0
CG C:ASP50 3.9 79.0 0.4
CE1 B:TYR179 3.9 78.7 0.4
CB C:SER53 4.0 64.2 0.4
CG2 B:VAL213 4.0 28.0 1.0
O C:HOH1492 4.4 67.0 1.0
CD2 B:TYR179 4.6 52.2 0.4
OE1 B:GLU131 4.6 40.2 1.0
CD1 B:TYR179 4.8 60.5 0.4
O C:ASP50 4.9 41.7 0.4
CG B:GLU212 4.9 26.5 1.0

Thallium binding site 4 out of 24 in 1f1h

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Thallium binding site 4 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 4 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Tl474

b:75.1
occ:0.39
 OE2 B:GLU131 2.7 32.2 1.0
O B:HOH1591 2.9 48.4 1.0
OD1 B:ASN264 3.0 65.7 1.0
O B:GLY265 3.1 36.4 1.0
O B:HOH1562 3.3 53.2 1.0
CD B:GLU131 3.4 37.3 1.0
OE1 B:GLU131 3.4 40.2 1.0
CG B:ASN264 4.0 53.5 1.0
C B:GLY265 4.2 25.4 1.0
N B:GLY267 4.2 35.8 1.0
OE1 B:GLU212 4.2 40.3 1.0
NE2 B:GLN218 4.3 15.7 1.0
OE1 B:GLN218 4.3 38.9 1.0
O B:HOH1580 4.5 34.4 1.0
O B:HOH1502 4.5 24.0 1.0
CA B:SER266 4.5 26.0 1.0
CD B:GLN218 4.8 15.3 1.0
CG B:GLU131 4.8 24.8 1.0
ND2 B:ASN264 4.8 31.9 1.0
C B:SER266 4.8 33.4 1.0
CB B:ASN264 4.8 49.0 1.0
CD B:GLU212 4.8 39.6 1.0
N B:SER266 4.8 25.7 1.0
N B:GLY265 4.9 28.7 1.0

Thallium binding site 5 out of 24 in 1f1h

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Thallium binding site 5 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 5 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Tl473

b:67.6
occ:0.39
 OH C:TYR179 2.9 86.1 0.4
OE2 C:GLU212 3.0 36.5 1.0
OG D:SER53 3.0 55.6 0.4
OD1 D:ASP50 3.1 81.2 0.4
OE1 C:GLU212 3.1 40.3 1.0
CZ C:TYR179 3.2 68.5 0.4
CD C:GLU212 3.4 39.6 1.0
O D:HOH1494 3.6 49.4 1.0
OD2 D:ASP50 3.6 76.7 0.4
CE2 C:TYR179 3.7 64.9 0.4
CB D:SER53 3.7 64.2 0.4
CG D:ASP50 3.8 79.0 0.4
MN C:MN469 3.8 34.9 1.0
CE1 C:TYR179 3.9 78.7 0.4
CG2 C:VAL213 4.0 28.0 1.0
O D:HOH1493 4.4 67.0 1.0
CD2 C:TYR179 4.6 52.2 0.4
OE1 C:GLU131 4.6 40.2 1.0
O D:ASP50 4.7 41.7 0.4
CD1 C:TYR179 4.8 60.5 0.4
CG C:GLU212 4.9 26.5 1.0

Thallium binding site 6 out of 24 in 1f1h

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Thallium binding site 6 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 6 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Tl474

b:75.1
occ:0.39
 OE2 C:GLU131 2.7 32.2 1.0
O C:HOH1591 2.9 48.4 1.0
OD1 C:ASN264 3.0 65.7 1.0
O C:GLY265 3.1 36.4 1.0
O C:HOH1563 3.3 53.2 1.0
CD C:GLU131 3.4 37.3 1.0
OE1 C:GLU131 3.4 40.2 1.0
CG C:ASN264 4.0 53.5 1.0
C C:GLY265 4.2 25.4 1.0
N C:GLY267 4.2 35.8 1.0
OE1 C:GLU212 4.2 40.3 1.0
NE2 C:GLN218 4.3 15.7 1.0
OE1 C:GLN218 4.3 38.9 1.0
O C:HOH1581 4.5 34.4 1.0
O C:HOH1504 4.5 24.0 1.0
CA C:SER266 4.5 26.0 1.0
CD C:GLN218 4.8 15.3 1.0
CG C:GLU131 4.8 24.8 1.0
ND2 C:ASN264 4.8 31.9 1.0
C C:SER266 4.8 33.4 1.0
CB C:ASN264 4.8 49.0 1.0
CD C:GLU212 4.8 39.6 1.0
N C:SER266 4.8 25.7 1.0
N C:GLY265 4.9 28.7 1.0

Thallium binding site 7 out of 24 in 1f1h

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Thallium binding site 7 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 7 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Tl473

b:67.6
occ:0.39
 OH D:TYR179 2.9 86.1 0.4
OE2 D:GLU212 3.0 36.5 1.0
OD1 E:ASP50 3.1 81.2 0.4
OG E:SER53 3.1 55.6 0.4
OE1 D:GLU212 3.1 40.3 1.0
CZ D:TYR179 3.2 68.5 0.4
CD D:GLU212 3.4 39.6 1.0
O D:HOH1595 3.6 49.4 1.0
OD2 E:ASP50 3.6 76.7 0.4
CE2 D:TYR179 3.7 64.9 0.4
CG E:ASP50 3.7 79.0 0.4
MN D:MN469 3.8 34.9 1.0
CB E:SER53 3.8 64.2 0.4
CE1 D:TYR179 3.9 78.7 0.4
CG2 D:VAL213 4.0 28.0 1.0
O E:HOH1493 4.4 67.0 1.0
CD2 D:TYR179 4.6 52.2 0.4
OE1 D:GLU131 4.6 40.2 1.0
O E:ASP50 4.7 41.7 0.4
CD1 D:TYR179 4.8 60.5 0.4
CG D:GLU212 4.9 26.5 1.0

Thallium binding site 8 out of 24 in 1f1h

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Thallium binding site 8 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 8 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Tl474

b:75.1
occ:0.39
 OE2 D:GLU131 2.7 32.2 1.0
O D:HOH1596 2.9 48.4 1.0
OD1 D:ASN264 3.0 65.7 1.0
O D:GLY265 3.1 36.4 1.0
O D:HOH1566 3.3 53.2 1.0
CD D:GLU131 3.4 37.3 1.0
OE1 D:GLU131 3.4 40.2 1.0
CG D:ASN264 4.0 53.5 1.0
C D:GLY265 4.2 25.4 1.0
N D:GLY267 4.2 35.8 1.0
OE1 D:GLU212 4.2 40.3 1.0
NE2 D:GLN218 4.3 15.7 1.0
OE1 D:GLN218 4.3 38.9 1.0
O D:HOH1585 4.5 34.4 1.0
O D:HOH1506 4.5 24.0 1.0
CA D:SER266 4.5 26.0 1.0
CD D:GLN218 4.8 15.3 1.0
CG D:GLU131 4.8 24.8 1.0
ND2 D:ASN264 4.8 31.9 1.0
C D:SER266 4.8 33.4 1.0
CB D:ASN264 4.8 49.0 1.0
CD D:GLU212 4.8 39.6 1.0
N D:SER266 4.8 25.7 1.0
N D:GLY265 4.9 28.7 1.0

Thallium binding site 9 out of 24 in 1f1h

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Thallium binding site 9 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 9 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Tl473

b:67.6
occ:0.39
 OH E:TYR179 2.9 86.1 0.4
OE2 E:GLU212 3.0 36.5 1.0
OE1 E:GLU212 3.1 40.3 1.0
CZ E:TYR179 3.2 68.5 0.4
OD1 F:ASP50 3.3 81.2 0.4
OG F:SER53 3.3 55.6 0.4
CD E:GLU212 3.4 39.6 1.0
O E:HOH1592 3.6 49.4 1.0
CE2 E:TYR179 3.7 64.9 0.4
OD2 F:ASP50 3.7 76.7 0.4
MN E:MN469 3.8 34.9 1.0
CG F:ASP50 3.9 79.0 0.4
CE1 E:TYR179 3.9 78.7 0.4
CG2 E:VAL213 4.0 28.0 1.0
CB F:SER53 4.0 64.2 0.4
O F:HOH1496 4.4 67.0 1.0
CD2 E:TYR179 4.6 52.2 0.4
OE1 E:GLU131 4.6 40.2 1.0
CD1 E:TYR179 4.8 60.5 0.4
CG E:GLU212 4.9 26.5 1.0
O F:ASP50 5.0 41.7 0.4

Thallium binding site 10 out of 24 in 1f1h

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Thallium binding site 10 out of 24 in the Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions


Mono view


Stereo pair view

A full contact list of Thallium with other atoms in the Tl binding site number 10 of Crystal Structure of Glutamine Synthetase From Salmonella Typhimurium with Thallium Ions within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Tl474

b:75.1
occ:0.39
 OE2 E:GLU131 2.7 32.2 1.0
O E:HOH1593 2.9 48.4 1.0
OD1 E:ASN264 3.0 65.7 1.0
O E:GLY265 3.1 36.4 1.0
O E:HOH1564 3.3 53.2 1.0
CD E:GLU131 3.4 37.3 1.0
OE1 E:GLU131 3.4 40.2 1.0
CG E:ASN264 4.0 53.5 1.0
C E:GLY265 4.2 25.4 1.0
N E:GLY267 4.2 35.8 1.0
OE1 E:GLU212 4.2 40.3 1.0
NE2 E:GLN218 4.3 15.7 1.0
OE1 E:GLN218 4.3 38.9 1.0
O E:HOH1582 4.5 34.4 1.0
O E:HOH1505 4.5 24.0 1.0
CA E:SER266 4.5 26.0 1.0
CD E:GLN218 4.8 15.3 1.0
CG E:GLU131 4.8 24.8 1.0
ND2 E:ASN264 4.8 31.9 1.0
C E:SER266 4.8 33.4 1.0
CB E:ASN264 4.8 49.0 1.0
CD E:GLU212 4.8 39.6 1.0
N E:SER266 4.8 25.7 1.0
N E:GLY265 4.9 28.7 1.0

Reference:

H.S.Gill, D.Eisenberg. The Crystal Structure of Phosphinothricin in the Active Site of Glutamine Synthetase Illuminates the Mechanism of Enzymatic Inhibition. Biochemistry V. 40 1903 2001.
ISSN: ISSN 0006-2960
PubMed: 11329256
DOI: 10.1021/BI002438H
Page generated: Wed Dec 16 02:28:36 2020

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