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Sodium in PDB 2xqk: X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S)

Enzymatic activity of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S)

All present enzymatic activity of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S):
3.1.1.8;

Protein crystallography data

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S), PDB code: 2xqk was solved by M.Wandhammer, E.Carletti, E.Gillon, P.Masson, M.Goeldner, D.Noort, F.Nachon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.53 / 2.40
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 154.920, 154.920, 127.390, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 21.7

Other elements in 2xqk:

The structure of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S) also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Calcium (Ca) 1 atom
Potassium (K) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S) (pdb code 2xqk). 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 X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S), PDB code: 2xqk:

Sodium binding site 1 out of 1 in 2xqk

Go back to Sodium Binding Sites List in 2xqk
Sodium binding site 1 out of 1 in the X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S)


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Structure of Human Butyrylcholinesterase Inhibited By Pure Enantiomer Vx-(S) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1535

b:42.9
occ:0.50
O A:HOH2059 2.5 33.6 1.0
OE1 A:GLU80 2.8 54.6 1.0
O A:HOH2055 2.9 20.8 1.0
O A:HOH2056 3.1 27.5 1.0
O A:HOH2043 3.4 29.7 1.0
CD A:GLU80 3.7 51.9 1.0
CG A:GLU80 4.4 44.5 1.0
OE2 A:GLU80 4.5 55.3 1.0
ND2 A:ASN83 4.6 35.5 1.0

Reference:

M.Wandhammer, E.Carletti, M.Van Der Schans, E.Gillon, Y.Nicolet, P.Masson, M.Goeldner, D.Noort, F.Nachon. Structural Study of the Complex Stereoselectivity of Human Butyrylcholinesterase For the Neurotoxic V-Agents. J.Biol.Chem. V. 286 16783 2011.
ISSN: ISSN 0021-9258
PubMed: 21454498
DOI: 10.1074/JBC.M110.209569
Page generated: Mon Oct 7 05:15:39 2024

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