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Cobalt in PDB 3urn: Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor

Enzymatic activity of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor

All present enzymatic activity of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor:
3.1.8.1;

Protein crystallography data

The structure of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor, PDB code: 3urn was solved by P.Tsai, N.G.Fox, Y.Li, D.P.Barondeau, F.M.Raushel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.81 / 1.95
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 85.498, 86.103, 88.741, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 24.7

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor (pdb code 3urn). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor, PDB code: 3urn:
Jump to Cobalt binding site number: 1; 2; 3; 4;

Cobalt binding site 1 out of 4 in 3urn

Go back to Cobalt Binding Sites List in 3urn
Cobalt binding site 1 out of 4 in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co801

b:21.3
occ:1.00
 NE2 A:HIS230 2.1 17.3 1.0
OQ2 A:KCX169 2.1 16.2 1.0
O A:HOH1361 2.1 18.4 1.0
ND1 A:HIS201 2.2 19.1 1.0
OAC A:QMP902 2.3 66.5 1.0
OAB A:QMP902 2.9 66.5 1.0
CE1 A:HIS201 3.0 21.7 1.0
CD2 A:HIS230 3.0 18.7 1.0
CX A:KCX169 3.0 19.2 1.0
CE1 A:HIS230 3.1 15.7 1.0
PAK A:QMP902 3.1 67.6 1.0
CG A:HIS201 3.3 20.6 1.0
OQ1 A:KCX169 3.3 19.0 1.0
CO A:CO802 3.7 21.5 1.0
CB A:HIS201 3.7 18.8 1.0
NE1 A:TRP131 4.0 24.8 1.0
ND1 A:HIS230 4.2 19.9 1.0
NE2 A:HIS55 4.2 21.1 1.0
CG A:HIS230 4.2 19.2 1.0
NE2 A:HIS201 4.2 22.4 1.0
OD2 A:ASP301 4.2 19.5 1.0
NZ A:KCX169 4.2 17.4 1.0
OAI A:QMP902 4.3 67.5 1.0
CD2 A:HIS201 4.4 23.2 1.0
CAA A:QMP902 4.4 67.5 1.0
CAJ A:QMP902 4.4 67.7 1.0
CE1 A:HIS55 4.5 22.9 1.0
CA A:HIS201 4.6 20.7 1.0
CD1 A:TRP131 4.7 23.6 1.0
CE A:KCX169 4.7 17.4 1.0
OD1 A:ASP301 5.0 21.4 1.0
CG A:ASP301 5.0 21.1 1.0

Cobalt binding site 2 out of 4 in 3urn

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Cobalt binding site 2 out of 4 in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co802

b:21.5
occ:1.00
 O A:HOH1361 1.8 18.4 1.0
NE2 A:HIS57 1.9 20.3 1.0
OQ1 A:KCX169 2.2 19.0 1.0
OD1 A:ASP301 2.3 21.4 1.0
NE2 A:HIS55 2.3 21.1 1.0
CE1 A:HIS57 2.9 21.3 1.0
CD2 A:HIS55 3.0 22.1 1.0
CD2 A:HIS57 3.0 20.7 1.0
CX A:KCX169 3.1 19.2 1.0
CG A:ASP301 3.1 21.1 1.0
CE1 A:HIS55 3.4 22.9 1.0
OD2 A:ASP301 3.4 19.5 1.0
OQ2 A:KCX169 3.6 16.2 1.0
CO A:CO801 3.7 21.3 1.0
ND1 A:HIS57 4.0 19.0 1.0
CG2 A:VAL101 4.0 20.6 1.0
CG A:HIS57 4.1 20.7 1.0
NZ A:KCX169 4.1 17.4 1.0
CAJ A:QMP902 4.1 67.7 1.0
CG A:HIS55 4.2 22.9 1.0
CE1 A:HIS230 4.2 15.7 1.0
CAE A:QMP902 4.3 67.6 1.0
ND1 A:HIS55 4.4 24.1 1.0
CAF A:QMP902 4.4 67.8 1.0
NE2 A:HIS230 4.4 17.3 1.0
CB A:ASP301 4.4 19.5 1.0
OAC A:QMP902 4.6 66.5 1.0
CAG A:QMP902 4.6 67.8 1.0
CAH A:QMP902 4.7 68.2 1.0
OAB A:QMP902 4.8 66.5 1.0
CA A:ASP301 4.8 20.8 1.0
CAD A:QMP902 4.9 67.6 1.0

Cobalt binding site 3 out of 4 in 3urn

Go back to Cobalt Binding Sites List in 3urn
Cobalt binding site 3 out of 4 in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co803

b:20.9
occ:1.00
 O B:HOH1368 1.9 13.6 1.0
NE2 B:HIS57 2.0 21.8 1.0
OQ2 B:KCX169 2.2 21.4 1.0
NE2 B:HIS55 2.3 22.8 1.0
OD1 B:ASP301 2.3 13.9 1.0
CD2 B:HIS55 3.0 21.1 1.0
CE1 B:HIS57 3.0 22.8 1.0
CX B:KCX169 3.0 21.6 1.0
CD2 B:HIS57 3.0 22.4 1.0
CG B:ASP301 3.1 15.4 1.0
OQ1 B:KCX169 3.3 25.0 1.0
CE1 B:HIS55 3.4 19.1 1.0
OD2 B:ASP301 3.4 19.8 1.0
OAC B:QMP901 3.8 70.7 1.0
CO B:CO804 3.8 24.9 1.0
CG2 B:VAL101 4.0 19.0 1.0
NZ B:KCX169 4.1 20.0 1.0
ND1 B:HIS57 4.1 19.4 1.0
CG B:HIS57 4.1 20.5 1.0
CAJ B:QMP901 4.2 71.1 1.0
CG B:HIS55 4.2 22.1 1.0
CE1 B:HIS230 4.2 23.1 1.0
ND1 B:HIS55 4.4 20.7 1.0
CB B:ASP301 4.5 17.9 1.0
CAF B:QMP901 4.5 71.1 1.0
NE2 B:HIS230 4.5 20.6 1.0
CAE B:QMP901 4.7 70.7 1.0
CAH B:QMP901 4.7 71.1 1.0
CAG B:QMP901 4.9 70.9 1.0
CA B:ASP301 4.9 20.8 1.0

Cobalt binding site 4 out of 4 in 3urn

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Cobalt binding site 4 out of 4 in the Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 4 of Crystal Structure of Pte Mutant H254G/H257W/L303T/K185R/I274N/A80V/S61T with Cyclohexyl Methylphosphonate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Co804

b:24.9
occ:1.00
 NE2 B:HIS230 2.1 20.6 1.0
ND1 B:HIS201 2.1 29.1 1.0
OAC B:QMP901 2.1 70.7 1.0
OQ1 B:KCX169 2.1 25.0 1.0
O B:HOH1368 2.4 13.6 1.0
CE1 B:HIS201 2.9 30.8 1.0
CE1 B:HIS230 3.0 23.1 1.0
CD2 B:HIS230 3.1 23.4 1.0
CX B:KCX169 3.2 21.6 1.0
CG B:HIS201 3.2 30.1 1.0
PAK B:QMP901 3.4 70.3 1.0
OQ2 B:KCX169 3.6 21.4 1.0
CB B:HIS201 3.6 26.4 1.0
CAA B:QMP901 3.7 70.4 1.0
CO B:CO803 3.8 20.9 1.0
NE1 B:TRP131 4.0 27.0 1.0
NE2 B:HIS201 4.1 31.1 1.0
ND1 B:HIS230 4.1 21.8 1.0
OAB B:QMP901 4.2 71.2 1.0
CG B:HIS230 4.2 22.0 1.0
CD2 B:HIS201 4.2 29.2 1.0
NE2 B:HIS55 4.3 22.8 1.0
NZ B:KCX169 4.3 20.0 1.0
OD2 B:ASP301 4.4 19.8 1.0
CE1 B:HIS55 4.5 19.1 1.0
CA B:HIS201 4.5 25.3 1.0
OAI B:QMP901 4.6 71.5 1.0
CD1 B:TRP131 4.6 26.4 1.0
CE B:KCX169 4.7 19.8 1.0
CAJ B:QMP901 4.7 71.1 1.0

Reference:

P.C.Tsai, N.Fox, A.N.Bigley, S.P.Harvey, D.P.Barondeau, F.M.Raushel. Enzymes For the Homeland Defense: Optimizing Phosphotriesterase For the Hydrolysis of Organophosphate Nerve Agents. Biochemistry V. 51 6463 2012.
ISSN: ISSN 0006-2960
PubMed: 22809162
DOI: 10.1021/BI300811T
Page generated: Tue Jul 30 16:46:10 2024

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