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Sodium in PDB 2wid: Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1

Enzymatic activity of Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1

All present enzymatic activity of Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1:
3.1.1.8;

Protein crystallography data

The structure of Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1, PDB code: 2wid was solved by E.Carletti, N.Aurbek, E.Gillon, M.Loiodice, Y.Nicolet, J.Fontecilla, P.Masson, H.Thiermann, F.Nachon, F.Worek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.84 / 2.30
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 155.038, 155.038, 126.206, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 25.5

Other elements in 2wid:

The structure of Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1 also contains other interesting chemical elements:

Chlorine (Cl) 5 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1 (pdb code 2wid). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1, PDB code: 2wid:

Sodium binding site 1 out of 1 in 2wid

Go back to Sodium Binding Sites List in 2wid
Sodium binding site 1 out of 1 in the Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Nonaged Form of Human Butyrylcholinesterase Inhibited By Tabun Analogue TA1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na602

b:63.8
occ:0.50
CZ A:PHE525 3.6 55.6 1.0
CE1 A:PHE525 3.8 55.0 1.0
CE2 A:PHE525 3.8 55.6 1.0
CE1 A:HIS372 4.2 35.5 0.5
CD1 A:PHE525 4.2 55.3 1.0
CD2 A:PHE525 4.2 54.6 1.0
CZ A:PHE364 4.3 31.1 1.0
CG A:PHE525 4.4 52.3 1.0
CB A:SER368 4.5 30.7 1.0
NE2 A:HIS372 4.9 33.9 0.5

Reference:

E.Carletti, N.Aurbek, E.Gillon, M.Loiodice, Y.Nicolet, J.C.Fontecilla-Camps, P.Masson, H.Thiermann, F.Nachon, F.Worek. Structure-Activity Analysis of Aging and Reactivation of Human Butyrylcholinesterase Inhibited By Analogues of Tabun. Biochem. J. V. 421 97 2009.
ISSN: ESSN 1470-8728
PubMed: 19368529
DOI: 10.1042/BJ20090091
Page generated: Tue Dec 15 05:57:39 2020

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