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Zinc in PDB 1p6b: X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T

Enzymatic activity of X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T

All present enzymatic activity of X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T:
3.1.8.1;

Protein crystallography data

The structure of X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T, PDB code: 1p6b 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 / 1.90
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 X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T (pdb code 1p6b). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T, PDB code: 1p6b:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 1p6b

Go back to Zinc Binding Sites List in 1p6b
Zinc binding site 1 out of 6 in the X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T


Mono view


Stereo pair view

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

b:21.7
occ:1.00
 NE2 A:HIS55 2.1 20.1 1.0
NE2 A:HIS57 2.1 15.0 1.0
O A:HOH14 2.2 17.7 1.0
OQ1 A:KCX169 2.3 26.6 1.0
OD1 A:ASP301 2.4 30.3 1.0
CD2 A:HIS55 2.9 17.9 1.0
CE1 A:HIS57 3.0 20.2 1.0
CD2 A:HIS57 3.2 19.6 1.0
CG A:ASP301 3.2 36.3 1.0
CE1 A:HIS55 3.2 21.0 1.0
CX A:KCX169 3.3 18.8 1.0
OD2 A:ASP301 3.4 21.1 1.0
OQ2 A:KCX169 3.8 30.0 1.0
O A:HOH15 4.0 22.6 1.0
CG A:HIS55 4.1 24.5 1.0
CG2 A:VAL101 4.2 13.2 1.0
ZN A:ZN402 4.2 23.1 1.0
ND1 A:HIS57 4.2 21.6 1.0
CE1 A:HIS230 4.2 25.6 1.0
ND1 A:HIS55 4.2 22.3 1.0
NZ A:KCX169 4.3 19.5 1.0
CG A:HIS57 4.3 11.9 1.0
CB A:ASP301 4.5 15.5 1.0
NE2 A:HIS230 4.6 20.4 1.0

Zinc binding site 2 out of 6 in 1p6b

Go back to Zinc Binding Sites List in 1p6b
Zinc binding site 2 out of 6 in the X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T


Mono view


Stereo pair view

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

b:23.1
occ:1.00
 OQ2 A:KCX169 1.8 30.0 1.0
O A:HOH15 2.0 22.6 1.0
NE2 A:HIS230 2.0 20.4 1.0
ND1 A:HIS201 2.1 17.1 1.0
CX A:KCX169 2.9 18.8 1.0
CE1 A:HIS230 3.0 25.6 1.0
CD2 A:HIS230 3.0 21.9 1.0
O A:HOH14 3.1 17.7 1.0
CG A:HIS201 3.1 24.2 1.0
CE1 A:HIS201 3.1 23.5 1.0
OQ1 A:KCX169 3.3 26.6 1.0
CB A:HIS201 3.3 23.6 1.0
O A:HOH464 3.7 50.5 1.0
NE1 A:TRP131 3.9 20.6 1.0
ND1 A:HIS230 4.1 26.5 1.0
CG A:HIS230 4.1 20.4 1.0
ZN A:ZN401 4.2 21.7 1.0
NZ A:KCX169 4.2 19.5 1.0
NE2 A:HIS201 4.3 24.8 1.0
CD2 A:HIS201 4.3 25.3 1.0
CA A:HIS201 4.3 16.5 1.0
CE1 A:HIS55 4.4 21.0 1.0
O A:HOH528 4.5 47.1 1.0
NE2 A:HIS55 4.6 20.1 1.0
CD1 A:TRP131 4.6 26.1 1.0
CE A:KCX169 4.6 29.1 1.0

Zinc binding site 3 out of 6 in 1p6b

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Zinc binding site 3 out of 6 in the X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn406

b:28.5
occ:1.00
 O A:HOH16 2.0 22.5 1.0
OD1 A:ASP253 2.0 18.7 1.0
ND1 A:HIS230 2.1 26.5 1.0
O A:HOH17 2.3 29.2 1.0
CE1 A:HIS230 3.0 25.6 1.0
CG A:HIS230 3.2 20.4 1.0
CG A:ASP253 3.2 28.6 1.0
CA A:HIS230 3.4 19.1 1.0
CB A:HIS230 3.6 16.0 1.0
OD2 A:ASP301 3.6 21.1 1.0
N A:GLY254 3.8 21.8 1.0
OD2 A:ASP253 3.9 21.5 1.0
CA A:GLY254 4.0 18.3 1.0
N A:HIS230 4.1 20.6 1.0
OD1 A:ASP232 4.1 23.4 1.0
C A:ASP253 4.1 20.9 1.0
NE2 A:HIS230 4.1 20.4 1.0
CD2 A:HIS230 4.2 21.9 1.0
OD1 A:ASP233 4.2 32.2 1.0
CB A:ASP253 4.3 14.9 1.0
CB A:ASP301 4.4 15.5 1.0
O A:ASP253 4.4 19.2 1.0
CG A:ASP301 4.4 36.3 1.0
OD2 A:ASP233 4.5 25.7 1.0
C A:HIS230 4.6 23.5 1.0
CA A:ASP253 4.6 18.3 1.0
CG A:ASP233 4.7 45.1 1.0
N A:ASP253 4.8 25.5 1.0
CG A:ASP232 5.0 24.6 1.0

Zinc binding site 4 out of 6 in 1p6b

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Zinc binding site 4 out of 6 in the X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn403

b:19.2
occ:1.00
 O B:HOH11 2.0 17.3 1.0
NE2 B:HIS55 2.1 19.1 1.0
NE2 B:HIS57 2.1 10.3 1.0
OQ2 B:KCX169 2.1 24.8 1.0
OD1 B:ASP301 2.4 17.8 1.0
CD2 B:HIS55 3.0 21.3 1.0
CD2 B:HIS57 3.1 7.6 1.0
CE1 B:HIS55 3.1 15.1 1.0
CE1 B:HIS57 3.1 14.9 1.0
CX B:KCX169 3.2 13.7 1.0
CG B:ASP301 3.2 15.8 1.0
OD2 B:ASP301 3.4 18.5 1.0
O B:HOH10 3.7 27.6 1.0
OQ1 B:KCX169 3.9 18.2 1.0
CG2 B:VAL101 4.1 10.5 1.0
NZ B:KCX169 4.1 18.7 1.0
CG B:HIS55 4.2 13.7 1.0
ND1 B:HIS55 4.2 12.5 1.0
CG B:HIS57 4.2 10.6 1.0
ZN B:ZN404 4.3 20.4 1.0
ND1 B:HIS57 4.3 16.2 1.0
CE1 B:HIS230 4.4 18.8 1.0
CB B:ASP301 4.6 12.1 1.0
NE2 B:HIS230 4.6 16.7 1.0
O B:HOH455 4.9 55.7 1.0

Zinc binding site 5 out of 6 in 1p6b

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Zinc binding site 5 out of 6 in the X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn404

b:20.4
occ:1.00
 OQ1 B:KCX169 1.9 18.2 1.0
ND1 B:HIS201 2.0 18.8 1.0
NE2 B:HIS230 2.1 16.7 1.0
O B:HOH10 2.7 27.6 1.0
CX B:KCX169 2.9 13.7 1.0
CE1 B:HIS201 2.9 19.3 1.0
CD2 B:HIS230 3.1 23.5 1.0
CG B:HIS201 3.1 18.0 1.0
O B:HOH473 3.2 31.4 1.0
CE1 B:HIS230 3.2 18.8 1.0
O B:HOH11 3.2 17.3 1.0
OQ2 B:KCX169 3.3 24.8 1.0
CB B:HIS201 3.5 8.9 1.0
NE1 B:TRP131 3.9 19.8 1.0
NE2 B:HIS201 4.1 21.1 1.0
NZ B:KCX169 4.2 18.7 1.0
CD2 B:HIS201 4.2 21.4 1.0
CG B:HIS230 4.2 20.0 1.0
ZN B:ZN403 4.3 19.2 1.0
ND1 B:HIS230 4.3 21.2 1.0
CA B:HIS201 4.5 15.2 1.0
O B:HOH531 4.5 58.5 1.0
CE B:KCX169 4.5 12.8 1.0
CE1 B:HIS55 4.6 15.1 1.0
CD1 B:TRP131 4.6 20.4 1.0
NE2 B:HIS55 4.8 19.1 1.0

Zinc binding site 6 out of 6 in 1p6b

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Zinc binding site 6 out of 6 in the X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of X-Ray Structure of Phosphotriesterase, Triple Mutant H254G/H257W/L303T within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn405

b:25.1
occ:1.00
 OD1 B:ASP253 2.0 21.6 1.0
ND1 B:HIS230 2.0 21.2 1.0
O B:HOH13 2.0 20.7 1.0
O B:HOH12 2.1 16.9 1.0
CE1 B:HIS230 2.7 18.8 1.0
CG B:ASP253 3.1 21.3 1.0
CG B:HIS230 3.2 20.0 1.0
CA B:HIS230 3.5 22.5 1.0
O B:HOH477 3.6 49.3 1.0
OD2 B:ASP301 3.6 18.5 1.0
CB B:HIS230 3.8 16.9 1.0
OD2 B:ASP253 3.8 16.9 1.0
N B:GLY254 3.8 22.7 1.0
OD1 B:ASP232 3.9 23.5 1.0
NE2 B:HIS230 4.0 16.7 1.0
N B:HIS230 4.1 12.0 1.0
CA B:GLY254 4.1 21.4 1.0
C B:ASP253 4.1 27.0 1.0
CD2 B:HIS230 4.2 23.5 1.0
CB B:ASP253 4.3 21.1 1.0
OD1 B:ASP233 4.4 20.9 1.0
CG B:ASP301 4.4 15.8 1.0
CB B:ASP301 4.4 12.1 1.0
O B:ASP253 4.5 20.0 1.0
CA B:ASP253 4.6 21.6 1.0
OD2 B:ASP233 4.6 19.9 1.0
C B:HIS230 4.7 19.7 1.0
CG B:ASP233 4.8 21.0 1.0
N B:ASP253 4.8 19.5 1.0
CG B:ASP232 4.9 23.0 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 17:43:49 2024

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