Atomistry » Zinc » PDB 2nwp-2o6i » 2o4q
Atomistry »
  Zinc »
    PDB 2nwp-2o6i »
      2o4q »

Zinc in PDB 2o4q: Structure of Phosphotriesterase Mutant G60A

Enzymatic activity of Structure of Phosphotriesterase Mutant G60A

All present enzymatic activity of Structure of Phosphotriesterase Mutant G60A:
3.1.8.1;

Protein crystallography data

The structure of Structure of Phosphotriesterase Mutant G60A, PDB code: 2o4q was solved by J.Kim, U.A.Ramagopal, P.C.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) 31.64 / 1.95
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 55.295, 68.299, 90.030, 90.05, 100.42, 89.96
R / Rfree (%) 16.4 / 22.6

Other elements in 2o4q:

The structure of Structure of Phosphotriesterase Mutant G60A also contains other interesting chemical elements:

Arsenic (As) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Phosphotriesterase Mutant G60A (pdb code 2o4q). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the Structure of Phosphotriesterase Mutant G60A, PDB code: 2o4q:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Zinc binding site 1 out of 8 in 2o4q

Go back to Zinc Binding Sites List in 2o4q
Zinc binding site 1 out of 8 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2401

b:16.7
occ:1.00
 O1 A:CAC1 2.0 24.3 0.8
NE2 A:HIS55 2.0 6.1 1.0
OQ1 A:KCX169 2.1 12.4 1.0
NE2 A:HIS57 2.1 13.7 1.0
OD1 A:ASP301 2.1 16.4 1.0
CD2 A:HIS55 2.9 10.3 1.0
CG A:ASP301 3.0 15.6 1.0
CD2 A:HIS57 3.1 11.3 1.0
CE1 A:HIS55 3.1 12.1 1.0
CX A:KCX169 3.1 16.4 1.0
CE1 A:HIS57 3.1 10.9 1.0
OD2 A:ASP301 3.2 17.7 1.0
AS A:CAC1 3.3 22.2 0.8
OQ2 A:KCX169 3.6 17.2 1.0
C2 A:CAC1 3.9 12.0 0.8
O A:HOH2488 4.0 17.5 1.0
ZN A:ZN2402 4.0 18.6 1.0
CG A:HIS55 4.1 13.8 1.0
O2 A:CAC1 4.1 16.0 0.8
ND1 A:HIS55 4.1 10.6 1.0
CE1 A:HIS230 4.1 15.3 1.0
NZ A:KCX169 4.1 14.5 1.0
CG2 A:VAL101 4.2 8.6 1.0
ND1 A:HIS57 4.2 8.9 1.0
CG A:HIS57 4.2 10.0 1.0
CB A:ASP301 4.4 16.5 1.0
NE2 A:HIS230 4.5 14.3 1.0
O A:HOH2593 4.5 22.4 1.0
CA A:ASP301 4.8 14.6 1.0
C1 A:CAC1 5.0 20.1 0.8

Zinc binding site 2 out of 8 in 2o4q

Go back to Zinc Binding Sites List in 2o4q
Zinc binding site 2 out of 8 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2402

b:18.6
occ:1.00
 OQ2 A:KCX169 1.9 17.2 1.0
O2 A:CAC1 2.1 16.0 0.8
NE2 A:HIS230 2.1 14.3 1.0
ND1 A:HIS201 2.2 14.5 1.0
CX A:KCX169 3.0 16.4 1.0
CE1 A:HIS230 3.1 15.3 1.0
CE1 A:HIS201 3.1 17.9 1.0
CD2 A:HIS230 3.1 17.5 1.0
CG A:HIS201 3.2 13.2 1.0
AS A:CAC1 3.3 22.2 0.8
OQ1 A:KCX169 3.3 12.4 1.0
O1 A:CAC1 3.5 24.3 0.8
CB A:HIS201 3.5 13.8 1.0
O A:HOH2593 3.9 22.4 1.0
ZN A:ZN2401 4.0 16.7 1.0
NE1 A:TRP131 4.0 12.9 1.0
NZ A:KCX169 4.2 14.5 1.0
ND1 A:HIS230 4.2 16.7 1.0
NE2 A:HIS201 4.2 17.7 1.0
CG A:HIS230 4.2 15.8 1.0
CE1 A:HIS55 4.3 12.1 1.0
CD2 A:HIS201 4.3 16.1 1.0
CA A:HIS201 4.3 13.1 1.0
NE2 A:HIS55 4.4 6.1 1.0
OD2 A:ASP301 4.6 17.7 1.0
C2 A:CAC1 4.6 12.0 0.8
CD1 A:TRP131 4.6 14.4 1.0
CE A:KCX169 4.6 14.7 1.0
C1 A:CAC1 4.7 20.1 0.8

Zinc binding site 3 out of 8 in 2o4q

Go back to Zinc Binding Sites List in 2o4q
Zinc binding site 3 out of 8 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2403

b:18.6
occ:1.00
 O2 B:CAC2 2.1 22.6 0.7
OQ2 B:KCX169 2.1 15.0 1.0
NE2 B:HIS57 2.1 17.2 1.0
NE2 B:HIS55 2.2 14.2 1.0
OD1 B:ASP301 2.2 15.7 1.0
CD2 B:HIS55 3.0 12.4 1.0
CG B:ASP301 3.0 22.3 1.0
CX B:KCX169 3.1 16.6 1.0
CE1 B:HIS57 3.1 14.6 1.0
CD2 B:HIS57 3.1 19.6 1.0
OD2 B:ASP301 3.2 17.0 1.0
CE1 B:HIS55 3.2 18.0 1.0
AS B:CAC2 3.3 21.9 0.7
OQ1 B:KCX169 3.6 14.9 1.0
C1 B:CAC2 3.8 13.6 0.7
ZN B:ZN2404 3.9 22.6 1.0
O B:HOH2469 3.9 21.1 1.0
NZ B:KCX169 4.1 18.1 1.0
O1 B:CAC2 4.1 13.2 0.7
CE1 B:HIS230 4.2 18.4 1.0
CG B:HIS55 4.2 17.2 1.0
CG2 B:VAL101 4.2 15.2 1.0
ND1 B:HIS57 4.2 14.5 1.0
CG B:HIS57 4.3 12.9 1.0
ND1 B:HIS55 4.3 10.5 1.0
CB B:ASP301 4.4 15.6 1.0
NE2 B:HIS230 4.5 17.8 1.0
CA B:ASP301 4.9 15.8 1.0
C2 B:CAC2 5.0 17.7 0.7

Zinc binding site 4 out of 8 in 2o4q

Go back to Zinc Binding Sites List in 2o4q
Zinc binding site 4 out of 8 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2404

b:22.6
occ:1.00
 OQ1 B:KCX169 2.0 14.9 1.0
NE2 B:HIS230 2.1 17.8 1.0
O1 B:CAC2 2.1 13.2 0.7
ND1 B:HIS201 2.2 18.3 1.0
CX B:KCX169 3.0 16.6 1.0
CD2 B:HIS230 3.1 18.4 1.0
CE1 B:HIS201 3.1 16.9 1.0
CE1 B:HIS230 3.1 18.4 1.0
CG B:HIS201 3.2 24.3 1.0
AS B:CAC2 3.3 21.9 0.7
OQ2 B:KCX169 3.3 15.0 1.0
O2 B:CAC2 3.5 22.6 0.7
CB B:HIS201 3.5 21.4 1.0
ZN B:ZN2403 3.9 18.6 1.0
NE1 B:TRP131 3.9 12.8 1.0
NZ B:KCX169 4.2 18.1 1.0
CG B:HIS230 4.2 15.3 1.0
ND1 B:HIS230 4.2 16.1 1.0
NE2 B:HIS201 4.2 19.8 1.0
CD2 B:HIS201 4.3 19.0 1.0
CA B:HIS201 4.3 21.1 1.0
NE2 B:HIS55 4.4 14.2 1.0
CE1 B:HIS55 4.4 18.0 1.0
OD2 B:ASP301 4.5 17.0 1.0
CD1 B:TRP131 4.5 16.3 1.0
C1 B:CAC2 4.6 13.6 0.7
CE B:KCX169 4.6 17.6 1.0
C2 B:CAC2 4.8 17.7 0.7

Zinc binding site 5 out of 8 in 2o4q

Go back to Zinc Binding Sites List in 2o4q
Zinc binding site 5 out of 8 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Zn2405

b:14.1
occ:0.90
 O2 K:CAC3 1.9 25.6 0.8
OQ1 K:KCX169 2.0 13.8 1.0
NE2 K:HIS55 2.0 9.3 1.0
NE2 K:HIS57 2.1 9.1 1.0
OD1 K:ASP301 2.1 12.7 1.0
CD2 K:HIS55 2.9 8.2 1.0
CG K:ASP301 3.0 16.1 1.0
CD2 K:HIS57 3.1 12.4 1.0
CE1 K:HIS57 3.1 8.8 1.0
CX K:KCX169 3.1 13.2 1.0
CE1 K:HIS55 3.1 11.0 1.0
OD2 K:ASP301 3.2 15.2 1.0
AS K:CAC3 3.3 22.5 0.8
OQ2 K:KCX169 3.6 11.6 1.0
C1 K:CAC3 3.9 12.7 0.8
ZN K:ZN2406 3.9 19.0 1.0
NZ K:KCX169 4.1 16.0 1.0
O K:HOH2517 4.1 21.4 1.0
CG K:HIS55 4.1 12.4 1.0
O1 K:CAC3 4.2 12.7 0.8
CE1 K:HIS230 4.2 11.0 1.0
ND1 K:HIS55 4.2 9.1 1.0
ND1 K:HIS57 4.2 7.5 1.0
CG2 K:VAL101 4.2 11.3 1.0
CG K:HIS57 4.2 8.8 1.0
CB K:ASP301 4.4 16.2 1.0
NE2 K:HIS230 4.4 18.6 1.0
O K:HOH2672 4.5 23.2 1.0
CA K:ASP301 4.8 14.8 1.0
C2 K:CAC3 5.0 19.6 0.8

Zinc binding site 6 out of 8 in 2o4q

Go back to Zinc Binding Sites List in 2o4q
Zinc binding site 6 out of 8 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range:
probe atom residue distance (Å) B Occ
K:Zn2406

b:19.0
occ:1.00
 OQ2 K:KCX169 2.0 11.6 1.0
O1 K:CAC3 2.1 12.7 0.8
NE2 K:HIS230 2.1 18.6 1.0
ND1 K:HIS201 2.2 17.8 1.0
CX K:KCX169 3.0 13.2 1.0
CD2 K:HIS230 3.1 12.1 1.0
CE1 K:HIS201 3.1 17.0 1.0
CE1 K:HIS230 3.2 11.0 1.0
CG K:HIS201 3.2 14.6 1.0
OQ1 K:KCX169 3.3 13.8 1.0
AS K:CAC3 3.3 22.5 0.8
O2 K:CAC3 3.4 25.6 0.8
CB K:HIS201 3.6 13.7 1.0
O K:HOH2672 3.8 23.2 1.0
ZN K:ZN2405 3.9 14.1 0.9
NE1 K:TRP131 3.9 15.6 1.0
NZ K:KCX169 4.2 16.0 1.0
NE2 K:HIS201 4.2 20.7 1.0
CG K:HIS230 4.2 14.3 1.0
ND1 K:HIS230 4.3 15.3 1.0
CD2 K:HIS201 4.3 16.4 1.0
CE1 K:HIS55 4.3 11.0 1.0
CA K:HIS201 4.3 13.2 1.0
NE2 K:HIS55 4.4 9.3 1.0
C1 K:CAC3 4.5 12.7 0.8
OD2 K:ASP301 4.6 15.2 1.0
CE K:KCX169 4.6 13.6 1.0
CD1 K:TRP131 4.6 15.6 1.0
C2 K:CAC3 4.8 19.6 0.8

Zinc binding site 7 out of 8 in 2o4q

Go back to Zinc Binding Sites List in 2o4q
Zinc binding site 7 out of 8 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Zn2407

b:14.7
occ:0.80
 O2 P:CAC4 2.0 19.5 0.7
OD1 P:ASP301 2.1 16.2 1.0
NE2 P:HIS57 2.1 19.2 1.0
NE2 P:HIS55 2.1 13.0 1.0
OQ2 P:KCX169 2.2 16.0 1.0
CG P:ASP301 2.9 19.0 1.0
CD2 P:HIS55 3.0 16.6 1.0
CD2 P:HIS57 3.1 15.3 1.0
CX P:KCX169 3.1 11.7 1.0
OD2 P:ASP301 3.2 19.3 1.0
CE1 P:HIS57 3.2 12.4 1.0
CE1 P:HIS55 3.2 16.8 1.0
AS P:CAC4 3.3 20.9 0.7
OQ1 P:KCX169 3.6 16.9 1.0
C1 P:CAC4 3.9 10.9 0.7
O P:HOH2516 3.9 22.4 1.0
ZN P:ZN2408 3.9 19.7 0.9
NZ P:KCX169 4.1 14.6 1.0
CG2 P:VAL101 4.2 15.3 1.0
O1 P:CAC4 4.2 16.3 0.7
CG P:HIS55 4.2 19.2 1.0
CE1 P:HIS230 4.2 17.6 1.0
CG P:HIS57 4.2 12.2 1.0
ND1 P:HIS57 4.2 15.5 1.0
ND1 P:HIS55 4.3 12.7 1.0
CB P:ASP301 4.4 15.0 1.0
NE2 P:HIS230 4.5 18.3 1.0
O P:HOH2566 4.6 26.5 1.0
CA P:ASP301 4.9 15.0 1.0
C2 P:CAC4 4.9 21.5 0.7

Zinc binding site 8 out of 8 in 2o4q

Go back to Zinc Binding Sites List in 2o4q
Zinc binding site 8 out of 8 in the Structure of Phosphotriesterase Mutant G60A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Structure of Phosphotriesterase Mutant G60A within 5.0Å range:
probe atom residue distance (Å) B Occ
P:Zn2408

b:19.7
occ:0.90
 OQ1 P:KCX169 2.0 16.9 1.0
ND1 P:HIS201 2.1 17.2 1.0
O1 P:CAC4 2.1 16.3 0.7
NE2 P:HIS230 2.1 18.3 1.0
CX P:KCX169 3.0 11.7 1.0
CE1 P:HIS201 3.0 16.4 1.0
CE1 P:HIS230 3.1 17.6 1.0
CD2 P:HIS230 3.1 18.9 1.0
CG P:HIS201 3.1 23.2 1.0
AS P:CAC4 3.3 20.9 0.7
O2 P:CAC4 3.3 19.5 0.7
OQ2 P:KCX169 3.3 16.0 1.0
CB P:HIS201 3.5 20.1 1.0
ZN P:ZN2407 3.9 14.7 0.8
NE1 P:TRP131 3.9 13.1 1.0
O P:HOH2566 4.0 26.5 1.0
NE2 P:HIS201 4.1 18.3 1.0
NZ P:KCX169 4.1 14.6 1.0
ND1 P:HIS230 4.2 17.6 1.0
CD2 P:HIS201 4.2 18.3 1.0
CG P:HIS230 4.2 19.6 1.0
CA P:HIS201 4.3 20.5 1.0
CE1 P:HIS55 4.4 16.8 1.0
NE2 P:HIS55 4.4 13.0 1.0
OD2 P:ASP301 4.4 19.3 1.0
CD1 P:TRP131 4.5 15.3 1.0
C1 P:CAC4 4.6 10.9 0.7
CE P:KCX169 4.6 17.3 1.0
C2 P:CAC4 4.8 21.5 0.7

Reference:

J.Kim, P.C.Tsai, S.L.Chen, F.Himo, S.C.Almo, F.M.Raushel. Structure of Diethyl Phosphate Bound to the Binuclear Metal Center of Phosphotriesterase. Biochemistry V. 47 9497 2008.
ISSN: ISSN 0006-2960
PubMed: 18702530
DOI: 10.1021/BI800971V
Page generated: Thu Oct 17 02:26:52 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy