Chlorine in PDB 4wvf: Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1

The structure of Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1, PDB code: 4wvf was solved by Q.Sun, Y.Chook, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.80
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	105.909, 105.909, 305.526, 90.00, 90.00, 90.00
R / Rfree (%)	13.7 / 18.4

The structure of Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1 also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Magnesium	(Mg)	1 atom

The binding sites of Chlorine atom in the Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1 (pdb code 4wvf). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1, PDB code: 4wvf:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1


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 KPT276 in Complex with CRM1-Ran-RANBP1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1105 b:74.0 occ:1.00 O C:HOH1295 3.4 36.4 1.0 N C:GLU1009 3.5 32.7 1.0 CB C:THR1007 3.8 30.0 1.0 CB C:GLU1009 3.8 37.4 0.5 CB C:GLU1009 3.8 36.3 0.5 N C:SER1008 3.9 31.7 1.0 CB C:SER1008 4.0 39.6 1.0 OG1 C:THR1007 4.1 30.8 1.0 CA C:GLU1009 4.3 34.6 0.5 CA C:GLU1009 4.3 34.7 0.5 CA C:SER1008 4.3 34.6 1.0 C C:SER1008 4.3 33.6 1.0 O C:HOH1248 4.4 35.9 1.0 C C:THR1007 4.6 28.9 1.0 O C:HOH1238 4.6 62.5 1.0 OG C:SER1008 4.7 46.9 1.0 CA C:THR1007 4.7 28.6 1.0 CG2 C:THR1007 4.8 31.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1106 b:63.5 occ:1.00 O C:LYS605 3.1 40.9 1.0 N C:TYR608 3.3 34.4 1.0 CB C:TYR608 3.3 45.0 1.0 C C:CYS606 3.5 32.8 1.0 O C:HOH1233 3.5 63.1 1.0 CA C:CYS606 3.6 34.6 1.0 N C:LYS607 3.7 33.6 1.0 O C:CYS606 3.8 32.7 1.0 CA C:TYR608 3.9 39.7 1.0 C C:LYS605 3.9 36.7 1.0 N C:CYS606 4.1 33.6 1.0 O C:HOH1234 4.2 61.4 1.0 C C:LYS607 4.3 37.6 1.0 CD C:LYS567 4.4 51.7 1.0 CE C:LYS567 4.4 50.1 1.0 CD2 C:HIS609 4.5 40.9 1.0 CA C:LYS607 4.5 34.9 1.0 CG C:LYS607 4.5 39.6 1.0 NZ C:LYS567 4.5 64.7 1.0 CD C:LYS607 4.5 43.8 1.0 CG C:TYR608 4.6 53.3 1.0 N C:HIS609 4.7 40.5 1.0 O C:HOH1229 4.8 59.3 1.0 C C:TYR608 4.8 40.9 1.0 CE C:LYS607 5.0 46.5 1.0 CB C:CYS606 5.0 35.2 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of KPT276 in Complex with CRM1-Ran-RANBP1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1107 b:81.1 occ:1.00 O C:HOH1515 3.3 49.3 1.0 NE2 C:GLN62 3.3 47.2 1.0 O C:HOH1950 3.4 68.0 1.0 O C:PRO61 3.5 42.5 1.0 C C:PRO61 3.7 42.0 1.0 CB C:PRO61 3.9 48.3 1.0 CB C:ASN113 3.9 52.9 1.0 N C:GLN62 4.0 41.4 1.0 CB C:PHE65 4.1 37.6 1.0 CD2 C:PHE65 4.2 40.1 1.0 CA C:GLN62 4.2 40.1 1.0 N C:LEU114 4.2 43.4 1.0 CD C:GLN62 4.3 45.8 1.0 CD1 A:ILE81 4.3 42.9 1.0 CG2 A:ILE81 4.4 39.9 1.0 CB C:LEU114 4.4 40.8 1.0 CA C:PRO61 4.4 44.3 1.0 CG C:GLN62 4.4 44.5 1.0 CA C:LEU114 4.5 40.9 1.0 CG C:PHE65 4.6 36.2 1.0 C C:ASN113 4.6 44.9 1.0 ND2 C:ASN113 4.7 69.2 1.0 CG1 A:ILE81 4.8 37.7 1.0 CG C:ASN113 4.9 66.8 1.0 O C:HOH1856 4.9 71.1 1.0 CA C:ASN113 4.9 47.1 1.0 CB C:GLN62 5.0 43.0 1.0 CD1 C:LEU114 5.0 43.6 1.0

J.D.Haines, O.Herbin, B.De La Hera, O.G.Vidaurre, G.A.Moy, Q.Sun, H.Y.Fung, S.Albrecht, K.Alexandropoulos, D.Mccauley, Y.M.Chook, T.Kuhlmann, G.J.Kidd, S.Shacham, P.Casaccia. Nuclear Export Inhibitors Avert Progression in Preclinical Models of Inflammatory Demyelination. Nat.Neurosci. V. 18 511 2015.
ISSN: ISSN 1097-6256
PubMed: 25706475
DOI: 10.1038/NN.3953