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Zinc in PDB 1p6c: Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate

Enzymatic activity of Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate

All present enzymatic activity of Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate:
3.1.8.1;

Protein crystallography data

The structure of Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate, PDB code: 1p6c was solved by C.M.Hill, W.Li, J.B.Thoden, H.M.Holden, F.M.Raushel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 130.400, 91.900, 69.700, 90.00, 90.90, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate (pdb code 1p6c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate, PDB code: 1p6c:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1p6c

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Zinc binding site 1 out of 4 in the Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:23.2
occ:1.00
 NE2 A:HIS57 2.0 8.0 1.0
OQ1 A:KCX169 2.0 17.7 1.0
NE2 A:HIS55 2.0 22.8 1.0
O A:HOH456 2.0 21.7 1.0
OD1 A:ASP301 2.4 23.2 1.0
CE1 A:HIS57 2.9 17.4 1.0
CD2 A:HIS55 2.9 18.2 1.0
CX A:KCX169 3.0 29.6 1.0
CD2 A:HIS57 3.0 8.3 1.0
CE1 A:HIS55 3.1 23.7 1.0
CG A:ASP301 3.3 48.6 1.0
OQ2 A:KCX169 3.5 26.2 1.0
C6 A:DII7 3.5 64.8 1.0
ZN A:ZN402 3.6 28.9 1.0
OD2 A:ASP301 3.7 20.4 1.0
C4 A:DII7 3.9 53.3 1.0
NZ A:KCX169 3.9 15.7 1.0
ND1 A:HIS57 4.1 20.4 1.0
CG A:HIS55 4.1 17.4 1.0
CG A:HIS57 4.1 17.7 1.0
CG2 A:VAL101 4.2 16.9 1.0
ND1 A:HIS55 4.2 14.8 1.0
CE1 A:HIS230 4.2 31.8 1.0
O1 A:DII7 4.2 33.1 1.0
NE2 A:HIS230 4.4 35.6 1.0
CB A:ASP301 4.6 11.5 1.0
C7 A:DII7 4.8 62.8 1.0
O3 A:DII7 4.9 81.8 1.0
C5 A:DII7 4.9 51.7 1.0
P1 A:DII7 4.9 60.7 1.0

Zinc binding site 2 out of 4 in 1p6c

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Zinc binding site 2 out of 4 in the Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:28.9
occ:1.00
 OQ2 A:KCX169 1.8 26.2 1.0
NE2 A:HIS230 2.0 35.6 1.0
O A:HOH456 2.1 21.7 1.0
ND1 A:HIS201 2.1 24.3 1.0
O1 A:DII7 2.2 33.1 1.0
CX A:KCX169 2.7 29.6 1.0
CE1 A:HIS230 2.9 31.8 1.0
CD2 A:HIS230 3.0 33.7 1.0
OQ1 A:KCX169 3.0 17.7 1.0
CE1 A:HIS201 3.1 24.7 1.0
CG A:HIS201 3.2 28.3 1.0
P1 A:DII7 3.4 60.7 1.0
CB A:HIS201 3.6 16.8 1.0
ZN A:ZN401 3.6 23.2 1.0
C7 A:DII7 3.6 62.8 1.0
NE2 A:HIS55 4.1 22.8 1.0
CE1 A:HIS55 4.1 23.7 1.0
NZ A:KCX169 4.1 15.7 1.0
ND1 A:HIS230 4.1 31.0 1.0
CG A:HIS230 4.1 28.6 1.0
NE1 A:TRP131 4.2 22.7 1.0
NE2 A:HIS201 4.2 33.4 1.0
CD2 A:HIS201 4.3 26.0 1.0
O3 A:DII7 4.5 81.8 1.0
C4 A:DII7 4.5 53.3 1.0
OD2 A:ASP301 4.5 20.4 1.0
O2 A:DII7 4.6 0.0 1.0
CA A:HIS201 4.6 21.7 1.0
CE A:KCX169 4.8 24.1 1.0
C6 A:DII7 4.8 64.8 1.0
CD1 A:TRP131 4.9 31.4 1.0
OD1 A:ASP301 5.0 23.2 1.0

Zinc binding site 3 out of 4 in 1p6c

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Zinc binding site 3 out of 4 in the Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn403

b:23.9
occ:1.00
 OQ2 B:KCX169 1.9 16.5 1.0
O B:HOH16 2.0 26.8 1.0
NE2 B:HIS55 2.1 15.4 1.0
NE2 B:HIS57 2.2 21.1 1.0
OD1 B:ASP301 2.2 23.1 1.0
CX B:KCX169 3.0 15.8 1.0
CD2 B:HIS55 3.0 15.8 1.0
CE1 B:HIS55 3.1 16.4 1.0
CG B:ASP301 3.1 25.7 1.0
CE1 B:HIS57 3.1 22.2 1.0
CD2 B:HIS57 3.1 15.1 1.0
OD2 B:ASP301 3.5 22.9 1.0
ZN B:ZN404 3.7 27.9 1.0
OQ1 B:KCX169 3.7 20.6 1.0
CG2 B:VAL101 3.9 23.7 1.0
C3 B:DII8 4.1 68.2 1.0
C1 B:DII8 4.2 49.7 1.0
NZ B:KCX169 4.2 22.4 1.0
CG B:HIS55 4.2 20.5 1.0
CE1 B:HIS230 4.2 25.3 1.0
ND1 B:HIS55 4.2 21.7 1.0
CG B:HIS57 4.3 22.0 1.0
ND1 B:HIS57 4.3 20.8 1.0
NE2 B:HIS230 4.4 29.5 1.0
CB B:ASP301 4.5 21.9 1.0
O1 B:DII8 4.9 42.5 1.0
C7 B:DII8 4.9 0.0 1.0

Zinc binding site 4 out of 4 in 1p6c

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Zinc binding site 4 out of 4 in the Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Phosphotriesterase Triple Mutant H254G/H257W/L303T Complexed with Diisopropylmethylphosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn404

b:27.9
occ:1.00
 OQ1 B:KCX169 1.9 20.6 1.0
ND1 B:HIS201 2.0 15.6 1.0
NE2 B:HIS230 2.1 29.5 1.0
O B:HOH16 2.1 26.8 1.0
O1 B:DII8 2.7 42.5 1.0
CX B:KCX169 2.9 15.8 1.0
CE1 B:HIS201 2.9 28.5 1.0
CD2 B:HIS230 3.0 30.6 1.0
CE1 B:HIS230 3.1 25.3 1.0
CG B:HIS201 3.1 24.8 1.0
OQ2 B:KCX169 3.2 16.5 1.0
CB B:HIS201 3.6 19.3 1.0
ZN B:ZN403 3.7 23.9 1.0
C7 B:DII8 3.8 0.0 1.0
P1 B:DII8 3.8 78.7 1.0
NE2 B:HIS201 4.1 26.7 1.0
NZ B:KCX169 4.1 22.4 1.0
CG B:HIS230 4.2 29.0 1.0
CD2 B:HIS201 4.2 25.7 1.0
ND1 B:HIS230 4.2 30.4 1.0
NE1 B:TRP131 4.2 16.0 1.0
CE1 B:HIS55 4.3 16.4 1.0
NE2 B:HIS55 4.4 15.4 1.0
CA B:HIS201 4.5 21.6 1.0
OD2 B:ASP301 4.6 22.9 1.0
CE B:KCX169 4.6 20.1 1.0
C1 B:DII8 4.8 49.7 1.0
O2 B:DII8 4.8 0.0 1.0
CD1 B:TRP131 4.9 19.7 1.0
O3 B:DII8 5.0 0.0 1.0

Reference:

C.M.Hill, W.S.Li, J.B.Thoden, H.M.Holden, F.M.Raushel. Enhanced Degradation of Chemical Warfare Agents Through Molecular Engineering of the Phosphotriesterase Active Site. J.Am.Chem.Soc. V. 125 8990 2003.
ISSN: ISSN 0002-7863
PubMed: 15369336
DOI: 10.1021/JA0358798
Page generated: Wed Oct 16 17:43:52 2024

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