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Chlorine in PDB 5jq7: Crystal Structure of Ebola Glycoprotein in Complex with Toremifene

Protein crystallography data

The structure of Crystal Structure of Ebola Glycoprotein in Complex with Toremifene, PDB code: 5jq7 was solved by Y.Zhao, J.Ren, D.I.Stuart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.15 / 2.69
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 113.450, 113.450, 306.870, 90.00, 90.00, 120.00
R / Rfree (%) 20.3 / 24.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Ebola Glycoprotein in Complex with Toremifene (pdb code 5jq7). 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 Crystal Structure of Ebola Glycoprotein in Complex with Toremifene, PDB code: 5jq7:

Chlorine binding site 1 out of 1 in 5jq7

Go back to Chlorine Binding Sites List in 5jq7
Chlorine binding site 1 out of 1 in the Crystal Structure of Ebola Glycoprotein in Complex with Toremifene


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Ebola Glycoprotein in Complex with Toremifene within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl705

b:97.9
occ:1.00
CL B:T0R705 0.0 97.9 1.0
C9 B:T0R705 1.8 90.4 1.0
C4 B:T0R705 2.8 88.5 1.0
C2 B:T0R705 3.1 82.7 1.0
C15 B:T0R705 3.5 81.7 1.0
C6 B:T0R705 3.6 81.5 1.0
CD1 A:LEU184 3.7 66.2 1.0
C1 B:T0R705 3.8 78.5 1.0
C14 B:T0R705 3.8 71.2 1.0
CD2 A:LEU186 3.8 86.8 1.0
C5 B:T0R705 4.2 72.7 1.0
CD2 B:LEU558 4.4 71.1 1.0
C21 B:T0R705 4.6 83.3 1.0
CD2 B:LEU554 4.7 76.6 1.0
C16 B:T0R705 4.7 83.0 1.0
C3 B:T0R705 4.8 80.6 1.0
C20 B:T0R705 4.9 70.8 1.0

Reference:

Y.Zhao, J.Ren, K.Harlos, D.M.Jones, A.Zeltina, T.A.Bowden, S.Padilla-Parra, E.E.Fry, D.I.Stuart. Toremifene Interacts with and Destabilizes the Ebola Virus Glycoprotein. Nature V. 535 168 2016.
ISSN: ESSN 1476-4687
PubMed: 27362232
DOI: 10.1038/NATURE18615
Page generated: Sat Jul 12 03:43:01 2025

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