Fluorine in PDB 6xjr: Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq)

The structure of Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq), PDB code: 6xjr was solved by J.M.Baumhardt, Y.M.Chook, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.25 / 1.94
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	105.992, 105.992, 306.033, 90, 90, 90
R / Rfree (%)	19.4 / 22.6

The structure of Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq) also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq) (pdb code 6xjr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq), PDB code: 6xjr:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq) within 5.0Å range: probe atom residue distance (Å) B Occ C:F1101 b:82.3 occ:1.00 F19 C:K851101 0.0 82.3 1.0 C17 C:K851101 1.4 69.6 1.0 F20 C:K851101 2.2 73.0 1.0 F18 C:K851101 2.2 63.8 1.0 C13 C:K851101 2.4 61.8 1.0 HD23 C:LEU580 2.6 43.2 1.0 HB3 C:LYS579 2.8 46.6 1.0 C12 C:K851101 3.1 61.6 1.0 HD21 C:LEU580 3.2 43.2 1.0 C14 C:K851101 3.3 66.6 1.0 CD2 C:LEU580 3.3 36.0 1.0 HE2 C:PHE583 3.3 69.3 1.0 HG2 C:LYS579 3.4 57.9 1.0 HG13 C:VAL576 3.5 30.7 1.0 HG3 C:LYS579 3.5 57.9 1.0 HG C:LEU580 3.6 33.0 1.0 HG2 C:MET556 3.6 34.5 1.0 CB C:LYS579 3.6 38.8 1.0 CE2 C:PHE583 3.7 57.7 1.0 CG C:LYS579 3.7 48.2 1.0 H C:LEU580 3.7 52.8 1.0 N C:LEU580 3.8 43.9 1.0 O C:VAL576 3.9 35.2 1.0 HA C:LEU580 4.0 40.0 1.0 CG C:LEU580 4.0 27.5 1.0 HA C:VAL576 4.1 42.1 1.0 HD22 C:LEU580 4.1 43.2 1.0 HD2 C:PHE583 4.1 69.5 1.0 CD2 C:PHE583 4.1 57.9 1.0 C C:LYS579 4.1 50.3 1.0 HB2 C:LYS579 4.3 46.6 1.0 HG3 C:MET556 4.3 34.5 1.0 C11 C:K851101 4.4 74.2 1.0 CA C:LEU580 4.4 33.3 1.0 CZ C:PHE583 4.4 62.2 1.0 CG1 C:VAL576 4.4 25.5 1.0 HG21 C:VAL559 4.4 27.4 0.8 HG22 C:ILE555 4.4 32.3 1.0 CG C:MET556 4.4 28.6 1.0 C9 C:K851101 4.5 60.0 1.0 HZ C:PHE583 4.5 74.7 1.0 HG12 C:VAL576 4.5 30.7 1.0 CA C:LYS579 4.5 39.6 1.0 O C:LYS579 4.7 30.8 1.0 C C:VAL576 4.7 35.3 1.0 HA C:MET556 4.7 31.8 1.0 CB C:LEU580 4.8 25.4 1.0 CA C:VAL576 4.8 35.0 1.0 HG21 C:ILE555 4.8 32.3 1.0 HG22 C:VAL576 4.8 36.9 1.0 HG11 C:VAL559 4.8 31.2 0.2 C10 C:K851101 4.9 61.0 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq) within 5.0Å range: probe atom residue distance (Å) B Occ C:F1101 b:73.0 occ:1.00 F20 C:K851101 0.0 73.0 1.0 C17 C:K851101 1.4 69.6 1.0 F19 C:K851101 2.2 82.3 1.0 F18 C:K851101 2.2 63.8 1.0 C13 C:K851101 2.4 61.8 1.0 HG22 C:ILE555 2.5 32.3 1.0 HE2 C:PHE583 2.7 69.3 1.0 C14 C:K851101 2.7 66.6 1.0 HG2 C:MET556 2.9 34.5 1.0 HG3 C:MET556 3.0 34.5 1.0 HG21 C:ILE555 3.1 32.3 1.0 CG2 C:ILE555 3.2 26.8 1.0 HB C:ILE555 3.3 39.6 1.0 CG C:MET556 3.4 28.6 1.0 HA C:MET556 3.4 31.8 1.0 CE2 C:PHE583 3.5 57.7 1.0 C12 C:K851101 3.6 61.6 1.0 N C:MET556 3.7 25.2 1.0 CB C:ILE555 3.8 32.9 1.0 H C:MET556 3.8 30.4 1.0 CA C:MET556 3.9 26.4 1.0 HZ C:PHE583 3.9 74.7 1.0 C C:ILE555 4.0 17.7 1.0 HD23 C:LEU580 4.0 43.2 1.0 HG21 C:VAL559 4.0 27.4 0.8 HG23 C:ILE555 4.0 32.3 1.0 C9 C:K851101 4.1 60.0 1.0 CZ C:PHE583 4.1 62.2 1.0 HD21 C:LEU580 4.2 43.2 1.0 CB C:MET556 4.2 27.6 1.0 O C:ILE555 4.3 21.2 1.0 O C:ALA552 4.4 30.9 1.0 CD2 C:PHE583 4.4 57.9 1.0 HD2 C:PHE583 4.4 69.5 1.0 HG22 C:VAL559 4.5 27.4 0.8 HG2 C:LYS579 4.5 57.9 1.0 CA C:ILE555 4.5 27.7 1.0 CD2 C:LEU580 4.6 36.0 1.0 HG11 C:VAL559 4.6 34.7 0.8 HG13 C:VAL576 4.7 30.7 1.0 CG2 C:VAL559 4.7 22.7 0.8 C11 C:K851101 4.7 74.2 1.0 HB2 C:MET556 4.8 33.2 1.0 SD C:MET556 4.8 28.5 1.0 HB3 C:LYS579 4.8 46.6 1.0 HA C:ALA552 4.8 59.7 1.0 HD13 C:ILE555 4.8 86.4 1.0 HG3 C:LYS579 4.8 57.9 1.0 HB C:VAL559 4.8 30.1 0.2 HG11 C:VAL559 4.9 31.2 0.2 C10 C:K851101 4.9 61.0 1.0 HD12 C:ILE555 4.9 86.4 1.0 HB3 C:MET556 4.9 33.2 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq)


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Kpt-185 Bound to CRM1 (E582K, 537-Dltvk-541 to Glceq) within 5.0Å range: probe atom residue distance (Å) B Occ C:F1101 b:63.8 occ:1.00 F18 C:K851101 0.0 63.8 1.0 C17 C:K851101 1.4 69.6 1.0 F19 C:K851101 2.2 82.3 1.0 F20 C:K851101 2.2 73.0 1.0 C13 C:K851101 2.4 61.8 1.0 HG13 C:VAL576 2.7 30.7 1.0 HG21 C:VAL559 2.8 27.4 0.8 C12 C:K851101 2.8 61.6 1.0 HG22 C:ILE555 2.9 32.3 1.0 HG11 C:VAL559 3.1 34.7 0.8 HG11 C:VAL559 3.3 31.2 0.2 HG22 C:VAL576 3.4 36.9 1.0 C14 C:K851101 3.6 66.6 1.0 HG21 C:VAL559 3.6 32.9 0.2 HG21 C:ILE555 3.7 32.3 1.0 CG2 C:VAL559 3.7 22.7 0.8 CG1 C:VAL576 3.7 25.5 1.0 CG2 C:ILE555 3.7 26.8 1.0 HB C:VAL559 3.8 30.1 0.2 HG22 C:VAL559 3.9 27.4 0.8 HA C:VAL576 3.9 42.1 1.0 CG1 C:VAL559 3.9 28.9 0.8 HG11 C:VAL576 4.0 30.7 1.0 HA C:MET556 4.0 31.8 1.0 HD21 C:LEU580 4.0 43.2 1.0 CG1 C:VAL559 4.1 25.9 0.2 HG13 C:VAL559 4.1 34.7 0.8 HG23 C:ILE555 4.1 32.3 1.0 C11 C:K851101 4.2 74.2 1.0 HG2 C:MET556 4.2 34.5 1.0 CG2 C:VAL576 4.2 30.7 1.0 HB3 C:LYS579 4.2 46.6 1.0 HD23 C:LEU580 4.2 43.2 1.0 HG12 C:VAL576 4.3 30.7 1.0 CB C:VAL559 4.3 25.0 0.2 CB C:VAL559 4.3 23.2 0.8 HG23 C:VAL559 4.3 27.4 0.8 CB C:VAL576 4.4 29.6 1.0 HG12 C:VAL559 4.4 31.2 0.2 CG2 C:VAL559 4.4 27.4 0.2 HB C:VAL559 4.4 27.9 0.8 HG21 C:VAL576 4.5 36.9 1.0 O C:ILE555 4.6 21.2 1.0 CA C:VAL576 4.6 35.0 1.0 CD2 C:LEU580 4.6 36.0 1.0 HG2 C:LYS579 4.6 57.9 1.0 HG12 C:VAL559 4.7 34.7 0.8 HG C:LEU580 4.7 33.0 1.0 C9 C:K851101 4.7 60.0 1.0 HE2 C:PHE583 4.7 69.3 1.0 C C:ILE555 4.8 17.7 1.0 O C:VAL576 4.8 35.2 1.0 HG23 C:VAL559 4.8 32.9 0.2 C16 C:K851101 4.8 71.7 1.0 HB C:ILE555 4.8 39.6 1.0 HG13 C:VAL559 4.9 31.2 0.2 HG3 C:MET556 4.9 34.5 1.0 CA C:MET556 4.9 26.4 1.0 CB C:ILE555 4.9 32.9 1.0 N C:MET556 4.9 25.2 1.0 CG C:MET556 4.9 28.6 1.0 C10 C:K851101 4.9 61.0 1.0 HG23 C:VAL576 5.0 36.9 1.0

J.S.Walker, Z.A.Hing, B.Harrington, J.Baumhardt, H.G.Ozer, A.Lehman, B.Giacopelli, L.Beaver, K.Williams, J.N.Skinner, C.B.Cempre, Q.Sun, S.Shacham, B.R.Stromberg, M.K.Summers, L.V.Abruzzo, L.Rassenti, T.J.Kipps, S.Parikh, N.E.Kay, K.A.Rogers, J.A.Woyach, V.Coppola, Y.M.Chook, C.Oakes, J.C.Byrd, R.Lapalombella. Recurrent XPO1 Mutations Alter Pathogenesis of Chronic Lymphocytic Leukemia. J Hematol Oncol V. 14 17 2021.
ISSN: ISSN 1756-8722
PubMed: 33451349
DOI: 10.1186/S13045-021-01032-2