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Zinc in PDB 1eyw: Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate

Enzymatic activity of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate

All present enzymatic activity of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate:
3.1.8.1;

Protein crystallography data

The structure of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate, PDB code: 1eyw was solved by H.M.Holden, M.M.Benning, F.M.Raushel, S.-B.Hong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 128.620, 92.330, 69.850, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate (pdb code 1eyw). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate, PDB code: 1eyw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1eyw

Go back to Zinc Binding Sites List in 1eyw
Zinc binding site 1 out of 2 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:9.9
occ:1.00
NE2 A:HIS55 2.0 5.9 1.0
NE2 A:HIS57 2.1 12.1 1.0
OQ2 A:KCX169 2.2 10.3 1.0
OD2 A:ASP301 2.2 8.2 1.0
O A:HOH410 2.2 19.6 1.0
CD2 A:HIS55 2.9 10.4 1.0
CE1 A:HIS57 3.1 12.5 1.0
CX A:KCX169 3.1 9.4 1.0
CD2 A:HIS57 3.1 8.0 1.0
CG A:ASP301 3.1 13.9 1.0
CE1 A:HIS55 3.2 10.9 1.0
OD1 A:ASP301 3.4 13.0 1.0
OQ1 A:KCX169 3.5 12.6 1.0
ZN A:ZN402 3.5 13.6 1.0
CG2 A:VAL101 4.1 6.7 1.0
CG A:HIS55 4.1 7.4 1.0
NZ A:KCX169 4.2 11.3 1.0
ND1 A:HIS55 4.2 7.9 1.0
ND1 A:HIS57 4.2 8.7 1.0
C3 A:TEN403 4.2 13.4 0.7
CE1 A:HIS230 4.2 8.3 1.0
CG A:HIS57 4.2 10.4 1.0
NE2 A:HIS230 4.3 13.0 1.0
CB A:ASP301 4.4 5.7 1.0
C4 A:TEN403 4.6 11.2 0.7
O1 A:TEN403 4.6 31.3 0.7
CA A:ASP301 4.9 8.4 1.0

Zinc binding site 2 out of 2 in 1eyw

Go back to Zinc Binding Sites List in 1eyw
Zinc binding site 2 out of 2 in the Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Three-Dimensional Structure of the Zinc-Containing Phosphotriesterase with Bound Substrate Analog Triethylphosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn402

b:13.6
occ:1.00
OQ1 A:KCX169 1.9 12.6 1.0
ND1 A:HIS201 2.0 22.0 1.0
NE2 A:HIS230 2.1 13.0 1.0
O A:HOH410 2.5 19.6 1.0
CX A:KCX169 2.9 9.4 1.0
CE1 A:HIS201 2.9 22.8 1.0
CD2 A:HIS230 3.1 6.8 1.0
CE1 A:HIS230 3.1 8.3 1.0
CG A:HIS201 3.2 19.9 1.0
OQ2 A:KCX169 3.3 10.3 1.0
O1 A:TEN403 3.4 31.3 0.7
ZN A:ZN401 3.5 9.9 1.0
CB A:HIS201 3.6 8.8 1.0
NE2 A:HIS55 4.0 5.9 1.0
CE1 A:HIS55 4.0 10.9 1.0
NE2 A:HIS201 4.1 17.7 1.0
CG A:HIS230 4.2 8.9 1.0
ND1 A:HIS230 4.2 9.6 1.0
CD2 A:HIS201 4.2 23.4 1.0
NZ A:KCX169 4.2 11.3 1.0
OD1 A:ASP301 4.2 13.0 1.0
NE1 A:TRP131 4.3 9.5 1.0
CA A:HIS201 4.4 13.0 1.0
P1 A:TEN403 4.7 36.3 0.7
CE A:KCX169 4.8 15.3 1.0
OD2 A:ASP301 4.8 8.2 1.0
O4 A:TEN403 4.8 34.7 0.7
CD1 A:TRP131 4.9 6.1 1.0
CG A:ASP301 4.9 13.9 1.0
C3 A:TEN403 4.9 13.4 0.7

Reference:

M.M.Benning, S.B.Hong, F.M.Raushel, H.M.Holden. The Binding of Substrate Analogs to Phosphotriesterase. J.Biol.Chem. V. 275 30556 2000.
ISSN: ISSN 0021-9258
PubMed: 10871616
DOI: 10.1074/JBC.M003852200
Page generated: Fri Sep 25 21:29:30 2020
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