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Atomistry » Chlorine » PDB 2vo6-2vv8 » 2vt7 » |
Chlorine in PDB 2vt7: Native Torpedo Californica Acetylcholinesterase Collected with A Cumulated Dose of 800000 GyEnzymatic activity of Native Torpedo Californica Acetylcholinesterase Collected with A Cumulated Dose of 800000 Gy
All present enzymatic activity of Native Torpedo Californica Acetylcholinesterase Collected with A Cumulated Dose of 800000 Gy:
3.1.1.7; Protein crystallography data
The structure of Native Torpedo Californica Acetylcholinesterase Collected with A Cumulated Dose of 800000 Gy, PDB code: 2vt7
was solved by
J.P.Colletier,
D.Bourgeois,
B.Sanson,
D.Fournier,
J.L.Sussman,
I.Silman,
M.Weik,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Native Torpedo Californica Acetylcholinesterase Collected with A Cumulated Dose of 800000 Gy
(pdb code 2vt7). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Native Torpedo Californica Acetylcholinesterase Collected with A Cumulated Dose of 800000 Gy, PDB code: 2vt7: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 2vt7Go back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Native Torpedo Californica Acetylcholinesterase Collected with A Cumulated Dose of 800000 Gy
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 2vt7Go back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Native Torpedo Californica Acetylcholinesterase Collected with A Cumulated Dose of 800000 Gy
![]() Mono view ![]() Stereo pair view
Reference:
J.P.Colletier,
D.Bourgeois,
B.Sanson,
D.Fournier,
J.L.Sussman,
I.Silman,
M.Weik.
Shoot-and-Trap: Use of Specific X-Ray Damage to Study Structural Protein Dynamics By Temperature-Controlled Cryo-Crystallography. Proc.Natl.Acad.Sci.Usa V. 105 11742 2008.
Page generated: Fri Jul 11 01:01:57 2025
ISSN: ISSN 0027-8424 PubMed: 18701720 DOI: 10.1073/PNAS.0804828105 |
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