Fluorine in PDB 6ohq: Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain

All present enzymatic activity of Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain:
3.1.4.4;

The structure of Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain, PDB code: 6ohq was solved by C.M.Metrick, J.V.Chodaparambil, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.32 / 2.69
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.227, 131.517, 106.414, 90.00, 112.05, 90.00
R / Rfree (%)	20.6 / 25.9

The binding sites of Fluorine atom in the Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain (pdb code 6ohq). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain, PDB code: 6ohq:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:F1001 b:48.6 occ:1.00 F1 A:MKA1001 0.0 48.6 1.0 C8 A:MKA1001 1.3 48.8 1.0 C7 A:MKA1001 2.3 48.5 1.0 CD1 A:MKA1001 2.4 49.0 1.0 C A:GLY410 3.3 47.1 1.0 O A:GLY410 3.4 46.4 1.0 CA A:GLY410 3.4 50.0 1.0 CG2 A:MKA1001 3.6 47.7 1.0 CG1 A:MKA1001 3.6 47.9 1.0 N A:GLY410 3.6 51.1 1.0 N A:ILE411 3.9 44.4 1.0 CB A:MKA1001 4.1 47.0 1.0 O A:TRP519 4.1 51.8 1.0 N A:TRP519 4.1 50.9 1.0 CB A:TRP519 4.3 45.2 1.0 CB A:ASP518 4.4 55.0 1.0 CA A:ILE411 4.5 41.2 1.0 CA A:TRP519 4.6 49.5 1.0 CE3 A:TRP519 4.7 40.7 1.0 C A:TRP519 4.7 52.5 1.0 CG2 A:ILE411 4.7 39.8 1.0 CG A:ASP518 4.8 57.1 1.0 C A:LEU409 4.8 51.8 1.0

Fluorine binding site 2 out of 2 in the Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Compound 4 Bound Human Phospholipase D2 Catalytic Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:F1001 b:60.5 occ:1.00 F1 B:MKA1001 0.0 60.5 1.0 C8 B:MKA1001 1.3 59.0 1.0 C7 B:MKA1001 2.3 57.4 1.0 CD1 B:MKA1001 2.3 58.4 1.0 CA B:GLY410 3.2 66.4 1.0 C B:GLY410 3.4 64.1 1.0 N B:GLY410 3.4 68.3 1.0 CG2 B:MKA1001 3.6 56.9 1.0 CG1 B:MKA1001 3.6 57.5 1.0 O B:GLY410 3.6 65.6 1.0 O B:TRP519 3.9 55.2 1.0 N B:TRP519 4.0 52.0 1.0 CB B:MKA1001 4.0 56.8 1.0 N B:ILE411 4.1 60.8 1.0 CB B:ASP518 4.2 57.3 1.0 CB B:TRP519 4.3 52.9 1.0 CA B:TRP519 4.5 53.1 1.0 C B:TRP519 4.6 54.1 1.0 CG B:ASP518 4.6 59.2 1.0 C B:LEU409 4.7 71.0 1.0 C B:ASP518 4.8 53.5 1.0 OD2 B:ASP518 4.8 59.9 1.0 CA B:ASP518 5.0 53.9 1.0

C.M.Metrick, E.A.Peterson, J.C.Santoro, I.J.Enyedy, P.Murugan, T.Chen, K.Michelsen, M.Cullivan, K.A.Spilker, P.R.Kumar, T.L.May-Dracka, J.V.Chodaparambil. Human Pld Structures Enable Drug Design and Characterization of Isoenzyme Selectivity. Nat.Chem.Biol. 2020.
ISSN: ESSN 1552-4469
PubMed: 32042197
DOI: 10.1038/S41589-019-0458-4