Atomistry » Zinc » PDB 1p1q-1pe7 » 1p6c
Atomistry »
  Zinc »
    PDB 1p1q-1pe7 »
      1p6c »

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

Go back to Zinc Binding Sites List in 1p6c
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

Go back to Zinc Binding Sites List in 1p6c
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

Go back to Zinc Binding Sites List in 1p6c
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

Go back to Zinc Binding Sites List in 1p6c
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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy