Fluorine in PDB 6j0o: Crystal Structure of Cert Start Domain in Complex with Compound SC1

The structure of Crystal Structure of Cert Start Domain in Complex with Compound SC1, PDB code: 6j0o was solved by M.Suzuki, N.Nakao, M.Ueno, S.Sakai, D.Egawa, H.Hanzawa, S.Kawasaki, K.Kumagai, S.Kobayashi, K.Hanada, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	60.250, 60.250, 153.550, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 24.3

The binding sites of Fluorine atom in the Crystal Structure of Cert Start Domain in Complex with Compound SC1 (pdb code 6j0o). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of Cert Start Domain in Complex with Compound SC1, PDB code: 6j0o:

Fluorine binding site 1 out of 1 in the Crystal Structure of Cert Start Domain in Complex with Compound SC1


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 Cert Start Domain in Complex with Compound SC1 within 5.0Å range: probe atom residue distance (Å) B Occ A:F600 b:28.2 occ:1.00 F1 A:XAF600 0.0 28.2 1.0 C9 A:XAF600 1.3 28.9 1.0 C10 A:XAF600 2.4 24.2 1.0 C8 A:XAF600 2.4 32.6 1.0 C1 A:XAF600 2.8 23.6 1.0 C6 A:XAF600 2.9 22.6 1.0 CG2 A:ILE523 3.5 16.7 1.0 C11 A:XAF600 3.7 24.5 1.0 C7 A:XAF600 3.7 26.9 1.0 NE2 A:HIS469 4.1 20.2 1.0 C2 A:XAF600 4.1 25.5 1.0 CB A:ALA521 4.2 20.2 1.0 C5 A:XAF600 4.2 20.2 1.0 CG1 A:VAL557 4.2 23.4 1.0 C12 A:XAF600 4.2 23.8 1.0 CD2 A:HIS469 4.3 21.2 1.0 CB A:VAL480 4.5 22.4 1.0 CG2 A:VAL480 4.6 17.7 1.0 CG1 A:VAL480 4.6 27.8 1.0 CG2 A:VAL557 4.7 21.4 1.0 CE1 A:HIS469 4.8 21.4 1.0 CB A:ILE523 4.9 15.9 1.0

N.Nakao, M.Ueno, S.Sakai, D.Egawa, H.Hanzawa, S.Kawasaki, K.Kumagai, M.Suzuki, S.Kobayashi, K.Hanada. Natural Ligand-Nonmimetic Inhibitors of the Lipid-Transfer Protein Cert Commun Chem 2019.
ISSN: ISSN 2399
DOI: 10.1038/S42004-019-0118-3