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Cobalt in PDB 3a3w: Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site

Enzymatic activity of Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site

All present enzymatic activity of Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site:
3.1.8.1;

Protein crystallography data

The structure of Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site, PDB code: 3a3w was solved by D.L.Ollis, D.S.Tawfik, G.Schenk, C.J.Jackson, J.L.Foo, N.Tokuriki, L.Afriat, P.D.Carr, H.K.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.80 / 1.85
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 109.011, 109.011, 62.689, 90.00, 90.00, 120.00
R / Rfree (%) 17.4 / 20.9

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site (pdb code 3a3w). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site, PDB code: 3a3w:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 3a3w

Go back to Cobalt Binding Sites List in 3a3w
Cobalt binding site 1 out of 2 in the Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co800

b:18.9
occ:1.00
 O A:HOH612 2.0 22.4 1.0
NE2 A:HIS57 2.1 17.6 1.0
NE2 A:HIS55 2.2 17.9 1.0
OD1 A:ASP301 2.2 16.0 1.0
OQ2 A:KCX169 2.2 21.9 1.0
CG A:ASP301 3.0 17.0 1.0
CD2 A:HIS55 3.0 14.6 1.0
CE1 A:HIS57 3.1 19.7 1.0
CD2 A:HIS57 3.1 17.5 1.0
CX A:KCX169 3.1 24.9 1.0
CE1 A:HIS55 3.2 14.7 1.0
OD2 A:ASP301 3.3 16.9 1.0
OQ1 A:KCX169 3.4 24.0 1.0
C11 A:EPL701 3.5 28.8 0.5
CO A:CO801 3.6 25.1 0.6
C10 A:EPL701 4.0 29.5 0.5
CG2 A:VAL101 4.1 15.6 1.0
ND1 A:HIS57 4.2 16.8 1.0
CG A:HIS57 4.2 15.3 1.0
NZ A:KCX169 4.2 21.4 1.0
CG A:HIS55 4.2 15.2 1.0
CE1 A:HIS230 4.3 24.2 1.0
ND1 A:HIS55 4.3 16.7 1.0
CB A:ASP301 4.4 16.1 1.0
NE2 A:HIS230 4.5 23.6 1.0
CA A:ASP301 4.8 15.2 1.0
O2 A:EPL701 4.9 33.1 0.5

Cobalt binding site 2 out of 2 in 3a3w

Go back to Cobalt Binding Sites List in 3a3w
Cobalt binding site 2 out of 2 in the Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Structure of Opda Mutant (G60A/A80V/S92A/R118Q/K185R/Q206P/D208G/I260T/G273S) with Diethyl 4-Methoxyphenyl Phosphate Bound in the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co801

b:25.1
occ:0.60
 OQ1 A:KCX169 2.0 24.0 1.0
NE2 A:HIS230 2.1 23.6 1.0
ND1 A:HIS201 2.1 28.2 1.0
O A:HOH612 2.2 22.4 1.0
CE1 A:HIS230 3.0 24.2 1.0
CX A:KCX169 3.0 24.9 1.0
CE1 A:HIS201 3.1 30.1 1.0
CD2 A:HIS230 3.1 26.1 1.0
CG A:HIS201 3.2 27.1 1.0
OQ2 A:KCX169 3.4 21.9 1.0
NH2 A:ARG254 3.5 36.0 1.0
CB A:HIS201 3.5 24.4 1.0
CO A:CO800 3.6 18.9 1.0
O1 A:EPL701 4.0 34.9 0.5
CE1 A:HIS55 4.1 14.7 1.0
NE2 A:HIS55 4.1 17.9 1.0
ND1 A:HIS230 4.1 25.3 1.0
NE1 A:TRP131 4.2 21.4 1.0
OD2 A:ASP301 4.2 16.9 1.0
CG A:HIS230 4.2 26.4 1.0
NZ A:KCX169 4.2 21.4 1.0
NE2 A:HIS201 4.2 30.8 1.0
CD2 A:HIS201 4.3 28.4 1.0
CA A:HIS201 4.4 24.6 1.0
CZ A:ARG254 4.5 37.5 1.0
CD1 A:TRP131 4.7 20.9 1.0
CE A:KCX169 4.7 21.9 1.0
C10 A:EPL701 4.8 29.5 0.5
CG A:ASP301 4.9 17.0 1.0
OD1 A:ASP301 5.0 16.0 1.0
O2 A:EPL701 5.0 33.1 0.5

Reference:

C.J.Jackson, J.-L.Foo, N.Tokuriki, L.Afriat, P.D.Carr, H.-K.Kim, G.Schenk, D.S.Tawfik, D.L.Ollis. Conformational Sampling, Catalysis, and Evolution of the Bacterial Phosphotriesterase Proc.Natl.Acad.Sci.Usa 2009.
ISSN: ESSN 1091-6490
PubMed: 19966226
DOI: 10.1073/PNAS.0907548106
Page generated: Tue Jul 30 15:45:11 2024

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