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Arsenic in PDB 3m1r: The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168

Enzymatic activity of The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168

All present enzymatic activity of The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168:
3.5.3.8;

Protein crystallography data

The structure of The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168, PDB code: 3m1r was solved by K.Tan, L.Bigelow, D.Trevino, K.Buck, A.Joachimiak, Midwest Centerfor Structural Genomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.47 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 142.038, 118.980, 123.340, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 23

Other elements in 3m1r:

The structure of The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168 also contains other interesting chemical elements:

Calcium (Ca) 12 atoms
Chlorine (Cl) 9 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168 (pdb code 3m1r). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 4 binding sites of Arsenic where determined in the The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168, PDB code: 3m1r:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in 3m1r

Go back to Arsenic Binding Sites List in 3m1r
Arsenic binding site 1 out of 4 in the The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:As320

b:57.5
occ:0.49
 AS C:CAC320 0.0 57.5 0.5
O1 C:CAC320 1.6 33.9 0.5
O2 C:CAC320 1.6 30.8 0.5
C1 C:CAC320 2.0 0.9 0.5
C2 C:CAC320 2.0 15.3 0.5
C1 C:CAC320 2.4 16.3 0.5
AS C:CAC320 2.8 72.2 0.5
O1 C:CAC320 2.9 41.7 0.5
C2 C:CAC320 3.2 12.3 0.5
CG B:PHE294 4.2 29.6 1.0
CB B:PHE294 4.2 29.4 1.0
CG C:PHE294 4.2 30.9 1.0
CB C:PHE294 4.3 21.3 1.0
CG A:PHE294 4.4 34.1 1.0
CB A:PHE294 4.4 32.9 1.0
O2 C:CAC320 4.4 0.2 0.5
CD2 B:PHE294 4.6 32.1 1.0
CD2 C:PHE294 4.6 35.6 1.0
CD1 B:PHE294 4.6 33.7 1.0
CD1 C:PHE294 4.6 33.8 1.0
CD1 A:PHE294 4.7 42.7 1.0
CD2 A:PHE294 4.8 36.4 1.0
SE B:MSE297 4.9 47.9 0.9

Arsenic binding site 2 out of 4 in 3m1r

Go back to Arsenic Binding Sites List in 3m1r
Arsenic binding site 2 out of 4 in the The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:As320

b:72.2
occ:0.51
 AS C:CAC320 0.0 72.2 0.5
O2 C:CAC320 1.6 0.2 0.5
O1 C:CAC320 1.6 41.7 0.5
C2 C:CAC320 2.0 12.3 0.5
C1 C:CAC320 2.0 16.3 0.5
O1 C:CAC320 2.6 33.9 0.5
AS C:CAC320 2.8 57.5 0.5
C2 C:CAC320 2.9 15.3 0.5
O2 C:CAC320 3.0 30.8 0.5
O C:SER249 3.7 30.7 1.0
O A:SER249 3.8 30.3 1.0
O B:SER249 4.2 29.0 1.0
CA C:SER249 4.4 22.8 1.0
CE A:MSE297 4.5 20.8 1.0
C C:SER249 4.5 31.7 1.0
SE A:MSE297 4.6 47.1 0.9
C A:SER249 4.7 30.2 1.0
CB C:SER249 4.7 31.8 1.0
C1 C:CAC320 4.8 0.9 0.5
CA A:SER249 4.8 36.0 1.0
CA B:SER249 4.9 29.3 1.0
C B:SER249 5.0 27.5 1.0

Arsenic binding site 3 out of 4 in 3m1r

Go back to Arsenic Binding Sites List in 3m1r
Arsenic binding site 3 out of 4 in the The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:As320

b:0.5
occ:0.61
 AS E:CAC320 0.0 0.5 0.6
O2 E:CAC320 1.6 59.5 0.6
O1 E:CAC320 1.6 36.0 0.6
C1 E:CAC320 2.0 31.3 0.6
C2 E:CAC320 2.0 26.2 0.6
O1 E:CAC320 2.6 20.4 0.4
AS E:CAC320 2.7 48.4 0.4
C1 E:CAC320 2.7 20.7 0.4
C2 E:CAC320 2.8 15.5 0.4
O F:SER249 4.1 31.5 1.0
O D:SER249 4.1 36.1 1.0
O E:SER249 4.2 29.9 1.0
O2 E:CAC320 4.3 0.5 0.4
SE F:MSE297 4.7 39.9 0.8
CE F:MSE297 4.7 16.8 1.0
CA D:SER249 4.9 31.1 1.0
CE E:MSE297 4.9 17.5 1.0
CG F:PRO252 4.9 31.8 1.0
C F:SER249 4.9 26.8 1.0
CA F:SER249 4.9 29.7 1.0
SE E:MSE297 4.9 52.6 0.9
C D:SER249 4.9 33.8 1.0
CE D:MSE297 5.0 23.5 1.0
SE D:MSE297 5.0 40.4 0.7

Arsenic binding site 4 out of 4 in 3m1r

Go back to Arsenic Binding Sites List in 3m1r
Arsenic binding site 4 out of 4 in the The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168 within 5.0Å range:
probe atom residue distance (Å) B Occ
E:As320

b:48.4
occ:0.39
 AS E:CAC320 0.0 48.4 0.4
O2 E:CAC320 1.6 0.5 0.4
O1 E:CAC320 1.6 20.4 0.4
C2 E:CAC320 1.9 26.2 0.6
C2 E:CAC320 2.0 15.5 0.4
C1 E:CAC320 2.0 20.7 0.4
AS E:CAC320 2.7 0.5 0.6
C1 E:CAC320 3.0 31.3 0.6
O1 E:CAC320 3.1 36.0 0.6
CG F:PHE294 4.1 28.1 1.0
CG D:PHE294 4.1 36.7 1.0
CB D:PHE294 4.1 34.7 1.0
O2 E:CAC320 4.2 59.5 0.6
CG E:PHE294 4.2 38.8 1.0
CB F:PHE294 4.2 22.2 1.0
CB E:PHE294 4.2 34.3 1.0
CD2 D:PHE294 4.4 35.4 1.0
CD2 E:PHE294 4.4 37.6 1.0
CD2 F:PHE294 4.4 29.6 1.0
CD1 F:PHE294 4.5 31.2 1.0
CD1 D:PHE294 4.5 36.5 1.0
CD1 E:PHE294 4.7 42.5 1.0
SE F:MSE297 4.9 39.9 0.8
SE D:MSE297 5.0 40.4 0.7
CE2 D:PHE294 5.0 37.8 1.0

Reference:

K.Tan, L.Bigelow, K.Buck, A.Joachimiak. The Crystal Structure of Formimidoylglutamase From Bacillus Subtilis Subsp. Subtilis Str. 168 To Be Published.
Page generated: Sun Jul 6 23:27:35 2025

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