Chlorine in PDB 4q9m: Crystal Structure of Upps in Complex with Fpp and An Allosteric Inhibitor

The structure of Crystal Structure of Upps in Complex with Fpp and An Allosteric Inhibitor, PDB code: 4q9m was solved by S.Liu, X.Qiu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.85 / 2.06
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	91.850, 91.850, 155.540, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 20.5

The structure of Crystal Structure of Upps in Complex with Fpp and An Allosteric Inhibitor also contains other interesting chemical elements:

Cadmium

(Cd)

15 atoms

The binding sites of Chlorine atom in the Crystal Structure of Upps in Complex with Fpp and An Allosteric Inhibitor (pdb code 4q9m). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Upps in Complex with Fpp and An Allosteric Inhibitor, PDB code: 4q9m:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Upps in Complex with Fpp and An Allosteric Inhibitor


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 Upps in Complex with Fpp and An Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:34.1 occ:1.00 CL A:2ZW301 0.0 34.1 1.0 C12 A:2ZW301 1.7 22.6 1.0 C13 A:2ZW301 2.7 20.6 1.0 C11 A:2ZW301 2.7 19.6 1.0 H16 A:2ZW301 2.8 20.9 0.0 C21 A:2ZW301 3.1 25.1 1.0 C25 A:2ZW301 3.4 27.2 1.0 H12 A:2ZW301 3.6 24.2 0.0 CE A:MET49 3.7 21.6 1.0 C3 A:2ZW301 3.8 28.1 1.0 N3 A:2ZW301 3.8 24.1 1.0 O A:PHE94 3.8 24.2 1.0 CD2 A:TYR98 3.9 21.7 1.0 CA A:PRO91 3.9 18.4 1.0 CA A:TYR95 3.9 19.3 1.0 N22 A:2ZW301 3.9 29.0 1.0 C14 A:2ZW301 4.0 19.8 1.0 C16 A:2ZW301 4.0 20.5 1.0 C A:PHE94 4.0 23.5 1.0 N A:TYR95 4.1 19.1 1.0 CB A:TYR98 4.1 21.2 1.0 CG2 A:VAL99 4.2 22.2 1.0 C24 A:2ZW301 4.2 29.6 1.0 O A:PRO91 4.3 20.9 1.0 CB A:PRO91 4.4 19.4 1.0 CG A:TYR98 4.5 22.2 1.0 C15 A:2ZW301 4.5 21.0 1.0 O23 A:2ZW301 4.5 31.6 1.0 C A:PRO91 4.6 21.3 1.0 O A:TYR95 4.6 23.9 1.0 O3 A:2ZW301 4.7 30.0 1.0 O A:LEU90 4.7 19.8 1.0 C41 A:2ZW301 4.7 23.7 1.0 C A:TYR95 4.7 24.2 1.0 H17 A:2ZW301 4.8 19.9 0.0 CB A:PHE94 4.8 19.8 1.0 H19 A:2ZW301 4.9 20.4 0.0 N A:PRO91 4.9 18.7 1.0 CE2 A:TYR98 4.9 22.6 1.0 CA A:PHE94 5.0 18.7 1.0 CB A:TYR95 5.0 20.0 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Upps in Complex with Fpp and An Allosteric Inhibitor


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 Upps in Complex with Fpp and An Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:37.7 occ:1.00 CL B:2ZW301 0.0 37.7 1.0 C12 B:2ZW301 1.7 26.8 1.0 C13 B:2ZW301 2.7 25.5 1.0 C11 B:2ZW301 2.7 27.2 1.0 H16 B:2ZW301 2.8 26.0 0.0 C21 B:2ZW301 3.0 30.4 1.0 C25 B:2ZW301 3.5 31.4 1.0 H12 B:2ZW301 3.6 27.6 0.0 CE B:MET49 3.7 29.0 1.0 C3 B:2ZW301 3.8 32.3 1.0 N3 B:2ZW301 3.8 27.6 1.0 N22 B:2ZW301 3.8 33.3 1.0 O B:PHE94 3.9 30.5 1.0 CA B:PRO91 3.9 23.1 1.0 CA B:TYR95 3.9 25.5 1.0 CD2 B:TYR98 4.0 31.4 1.0 C14 B:2ZW301 4.0 25.1 1.0 C16 B:2ZW301 4.0 24.8 1.0 C B:PHE94 4.1 31.1 1.0 N B:TYR95 4.1 26.0 1.0 CB B:TYR98 4.2 27.6 1.0 CG2 B:VAL99 4.2 22.7 1.0 O B:PRO91 4.3 28.6 1.0 CB B:PRO91 4.3 22.7 1.0 C24 B:2ZW301 4.3 33.8 1.0 C15 B:2ZW301 4.5 23.3 1.0 CG B:TYR98 4.5 31.1 1.0 O23 B:2ZW301 4.5 35.3 1.0 C B:PRO91 4.6 27.5 1.0 O3 B:2ZW301 4.6 36.9 1.0 O B:TYR95 4.6 29.7 1.0 C41 B:2ZW301 4.7 26.0 1.0 O B:LEU90 4.7 25.8 1.0 C B:TYR95 4.7 31.5 1.0 H17 B:2ZW301 4.8 25.3 0.0 N B:PRO91 4.9 23.2 1.0 H19 B:2ZW301 4.9 24.4 0.0 CB B:PHE94 4.9 30.1 1.0 CE2 B:TYR98 5.0 32.2 1.0 CB B:TYR95 5.0 25.9 1.0

D.E.Danley, E.T.Baima, M.Mansour, K.F.Fennell, B.A.Chrunyk, J.P.Mueller, S.Liu, X.Qiu. Discovery and Structural Characterization of An Allosteric Inhibitor of Bacterial Cis-Prenyltransferase. Protein Sci. 2014.
ISSN: ESSN 1469-896X
PubMed: 25287857
DOI: 10.1002/PRO.2579