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Chlorine in PDB 3dl7: Aged Form of Mouse Acetylcholinesterase Inhibited By Tabun- Update

Enzymatic activity of Aged Form of Mouse Acetylcholinesterase Inhibited By Tabun- Update

All present enzymatic activity of Aged Form of Mouse Acetylcholinesterase Inhibited By Tabun- Update:
3.1.1.7;

Protein crystallography data

The structure of Aged Form of Mouse Acetylcholinesterase Inhibited By Tabun- Update, PDB code: 3dl7 was solved by E.Carletti, H.Li, B.Li, F.Ekstrom, Y.Nicolet, M.Loiodice, E.Gillon, M.T.Froment, O.Lockridge, L.M.Schopfer, P.Masson, F.Nachon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.82 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.020, 110.880, 226.380, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 22.7

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Aged Form of Mouse Acetylcholinesterase Inhibited By Tabun- Update (pdb code 3dl7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Aged Form of Mouse Acetylcholinesterase Inhibited By Tabun- Update, PDB code: 3dl7:

Chlorine binding site 1 out of 1 in 3dl7

Go back to Chlorine Binding Sites List in 3dl7
Chlorine binding site 1 out of 1 in the Aged Form of Mouse Acetylcholinesterase Inhibited By Tabun- Update


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Aged Form of Mouse Acetylcholinesterase Inhibited By Tabun- Update within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl550

b:87.4
occ:1.00
O A:HOH786 3.3 53.8 1.0
CD1 A:ILE429 3.3 43.7 1.0
NH1 A:ARG525 3.4 63.6 1.0
OE2 A:GLU431 4.3 47.1 1.0
CD A:LYS332 4.5 50.8 1.0
CZ A:ARG525 4.6 63.5 1.0
NH1 A:ARG521 4.8 45.3 1.0
CG A:LYS332 4.8 46.0 1.0
CG1 A:ILE429 4.8 43.3 1.0

Reference:

E.Carletti, H.Li, B.Li, F.Ekstrom, Y.Nicolet, M.Loiodice, E.Gillon, M.T.Froment, O.Lockridge, L.M.Schopfer, P.Masson, F.Nachon. Aging of Cholinesterases Phosphylated By Tabun Proceeds Through O-Dealkylation. J.Am.Chem.Soc. V. 130 16011 2008.
ISSN: ISSN 0002-7863
PubMed: 18975951
DOI: 10.1021/JA804941Z
Page generated: Sat Jul 20 18:21:21 2024

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