Atomistry » Arsenic » PDB 2im3-2xnq » 2o4m
Atomistry »
  Arsenic »
    PDB 2im3-2xnq »
      2o4m »

Arsenic in PDB 2o4m: Structure of Phosphotriesterase Mutant I106G/F132G/H257Y

Enzymatic activity of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y

All present enzymatic activity of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y:
3.1.8.1;

Protein crystallography data

The structure of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y, PDB code: 2o4m was solved by J.Kim, U.A.Ramagopal, P.Tsai, F.M.Raushel, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.33 / 1.64
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 56.759, 68.906, 89.670, 90.03, 100.29, 94.12
R / Rfree (%) 18.9 / 24.4

Other elements in 2o4m:

The structure of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y also contains other interesting chemical elements:

Zinc (Zn) 23 atoms

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y (pdb code 2o4m). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 4 binding sites of Arsenic where determined in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y, PDB code: 2o4m:
Jump to Arsenic binding site number: 1; 2; 3; 4;

Arsenic binding site 1 out of 4 in 2o4m

Go back to Arsenic Binding Sites List in 2o4m
Arsenic binding site 1 out of 4 in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As4001

b:12.5
occ:0.80
AS A:CAC4001 0.0 12.5 0.8
O2 A:CAC4001 1.7 7.1 0.8
O1 A:CAC4001 1.8 14.0 0.8
C2 A:CAC4001 2.0 15.3 0.8
C1 A:CAC4001 2.0 10.7 0.8
ZN A:ZN3003 3.1 10.6 0.8
ZN A:ZN3001 3.2 9.8 0.8
OQ1 A:KCX169 3.5 11.7 1.0
OD2 A:ASP301 3.8 12.4 1.0
O A:HOH6413 4.1 32.2 1.0
OQ2 A:KCX169 4.1 14.0 1.0
NE2 A:HIS230 4.2 13.8 1.0
CX A:KCX169 4.3 15.7 1.0
NE1 A:TRP131 4.3 18.1 1.0
NE2 A:HIS57 4.3 11.0 1.0
OD1 A:ASP301 4.4 10.4 1.0
CG A:ASP301 4.5 13.4 1.0
CZ2 A:TRP131 4.6 18.5 1.0
CE1 A:HIS230 4.6 13.1 1.0
ND1 A:HIS201 4.6 7.3 1.0
CE2 A:TRP131 4.8 18.7 1.0
CE1 A:HIS57 4.8 11.3 1.0
NE2 A:HIS55 4.9 12.2 1.0
CE1 A:HIS201 4.9 20.0 1.0

Arsenic binding site 2 out of 4 in 2o4m

Go back to Arsenic Binding Sites List in 2o4m
Arsenic binding site 2 out of 4 in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As4002

b:15.2
occ:0.80
AS B:CAC4002 0.0 15.2 0.8
O1 B:CAC4002 1.7 8.9 0.8
O2 B:CAC4002 1.8 16.1 0.8
C1 B:CAC4002 2.0 18.6 0.8
C2 B:CAC4002 2.0 18.1 0.8
ZN B:ZN3006 3.1 14.1 0.9
ZN B:ZN3005 3.2 12.0 0.9
OQ2 B:KCX169 3.4 12.6 1.0
OD2 B:ASP301 3.8 13.8 1.0
O B:HOH6162 4.1 22.3 1.0
OQ1 B:KCX169 4.1 15.7 1.0
NE1 B:TRP131 4.2 23.9 1.0
CX B:KCX169 4.2 14.5 1.0
NE2 B:HIS230 4.2 12.6 1.0
CH3 B:ACY6002 4.2 39.0 1.0
NE2 B:HIS57 4.3 8.5 1.0
OD1 B:ASP301 4.3 12.8 1.0
CG B:ASP301 4.5 20.1 1.0
CZ2 B:TRP131 4.6 25.6 1.0
CE1 B:HIS230 4.6 14.4 1.0
ND1 B:HIS201 4.7 16.2 1.0
CE2 B:TRP131 4.7 21.9 1.0
CE1 B:HIS57 4.8 14.1 1.0
NE2 B:HIS55 4.9 11.4 1.0
CE1 B:HIS201 4.9 19.5 1.0

Arsenic binding site 3 out of 4 in 2o4m

Go back to Arsenic Binding Sites List in 2o4m
Arsenic binding site 3 out of 4 in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y within 5.0Å range:
probe atom residue distance (Å) B Occ
C:As4003

b:13.9
occ:0.75
AS C:CAC4003 0.0 13.9 0.8
O2 C:CAC4003 1.7 8.8 0.8
O1 C:CAC4003 1.7 18.2 0.8
C2 C:CAC4003 1.9 24.0 0.8
C1 C:CAC4003 1.9 14.5 0.8
ZN C:ZN3008 3.1 14.2 0.9
ZN C:ZN3007 3.3 12.1 0.9
OQ1 C:KCX169 3.6 16.3 1.0
OD2 C:ASP301 3.8 13.8 1.0
O C:HOH6288 3.8 28.4 1.0
OQ2 C:KCX169 4.1 15.7 1.0
CX C:KCX169 4.3 14.8 1.0
NE2 C:HIS230 4.3 14.7 1.0
NE1 C:TRP131 4.3 25.1 1.0
NE2 C:HIS57 4.3 9.8 1.0
OD1 C:ASP301 4.4 12.0 1.0
CG C:ASP301 4.5 16.0 1.0
ND1 C:HIS201 4.6 12.5 1.0
CZ2 C:TRP131 4.7 20.0 1.0
CE1 C:HIS230 4.7 11.8 1.0
CE2 C:TRP131 4.8 18.3 1.0
CE1 C:HIS57 4.9 12.6 1.0
NE2 C:HIS55 4.9 11.8 1.0
CE1 C:HIS201 5.0 20.4 1.0

Arsenic binding site 4 out of 4 in 2o4m

Go back to Arsenic Binding Sites List in 2o4m
Arsenic binding site 4 out of 4 in the Structure of Phosphotriesterase Mutant I106G/F132G/H257Y


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of Structure of Phosphotriesterase Mutant I106G/F132G/H257Y within 5.0Å range:
probe atom residue distance (Å) B Occ
P:As4004

b:13.4
occ:0.80
AS P:CAC4004 0.0 13.4 0.8
O2 P:CAC4004 1.7 7.4 0.8
O1 P:CAC4004 1.7 14.6 0.8
C2 P:CAC4004 1.9 16.0 0.8
C1 P:CAC4004 2.0 16.2 0.8
ZN P:ZN3004 3.1 10.9 0.8
ZN P:ZN3002 3.3 8.9 0.8
OQ2 P:KCX169 3.6 16.5 1.0
OD2 P:ASP301 3.7 13.0 1.0
OQ1 P:KCX169 4.1 15.3 1.0
O P:HOH5140 4.2 27.5 1.0
CX P:KCX169 4.3 18.7 1.0
NE2 P:HIS230 4.3 13.5 1.0
OD1 P:ASP301 4.4 12.4 1.0
NE2 P:HIS57 4.4 9.7 1.0
NE1 P:TRP131 4.5 29.4 1.0
CG P:ASP301 4.5 13.4 1.0
O2 P:GOL5003 4.6 35.7 1.0
CE1 P:HIS230 4.7 11.3 1.0
ND1 P:HIS201 4.7 14.1 1.0
CZ2 P:TRP131 4.8 26.5 1.0
CE1 P:HIS57 4.9 10.7 1.0
NE2 P:HIS55 4.9 9.7 1.0
CE1 P:HIS201 4.9 21.4 1.0
CE2 P:TRP131 5.0 29.2 1.0

Reference:

J.Kim, U.A.Ramagopal, P.Tsai, F.M.Raushel, S.C.Almo. Structure of Phosphotriesterase Mutant I106G/F132G/H257Y To Be Published.
Page generated: Tue Oct 27 16:49:13 2020

Last articles

Xe in 6AYK
Xe in 6QII
Xe in 6ASM
Xe in 5NSW
Xe in 6FY9
Xe in 5O1K
Xe in 5O27
Xe in 5M69
Xe in 5KPU
Xe in 5I63
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy