Chlorine in PDB 8bjd: Full Length Structure of Lpmip with Bound Inhibitor JK095

All present enzymatic activity of Full Length Structure of Lpmip with Bound Inhibitor JK095:
5.2.1.8;

The structure of Full Length Structure of Lpmip with Bound Inhibitor JK095, PDB code: 8bjd was solved by J.J.Whittaker, A.Guskov, B.Goretzki, U.A.Hellmich, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.24 / 2.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	76.752, 76.752, 103.597, 90, 90, 90
R / Rfree (%)	24.6 / 29.4

The structure of Full Length Structure of Lpmip with Bound Inhibitor JK095 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Full Length Structure of Lpmip with Bound Inhibitor JK095 (pdb code 8bjd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Full Length Structure of Lpmip with Bound Inhibitor JK095, PDB code: 8bjd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Full Length Structure of Lpmip with Bound Inhibitor JK095


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Full Length Structure of Lpmip with Bound Inhibitor JK095 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:61.9 occ:1.00 CL1 A:9QN301 0.0 61.9 1.0 CAP A:9QN301 1.7 55.8 1.0 CAQ A:9QN301 2.7 54.6 1.0 CAO A:9QN301 2.7 48.3 1.0 CD1 A:ILE194 3.8 44.9 1.0 NH2 A:ARG188 3.9 65.8 1.0 CZ A:ARG188 3.9 63.0 1.0 CZ A:TYR185 4.0 45.7 1.0 CAR A:9QN301 4.0 55.7 1.0 CAN A:9QN301 4.0 50.2 1.0 NE A:ARG188 4.0 63.4 1.0 CG1 A:ILE194 4.1 41.2 1.0 OH A:TYR185 4.1 50.0 1.0 CE2 A:TYR185 4.1 42.0 1.0 CE1 A:TYR185 4.3 44.9 1.0 CG A:PRO193 4.4 54.6 1.0 CAS A:9QN301 4.5 52.7 1.0 CB A:ILE194 4.5 51.4 1.0 NH1 A:ARG188 4.6 59.8 1.0 CD2 A:TYR185 4.6 38.2 1.0 CD A:ARG188 4.7 62.6 1.0 CD1 A:TYR185 4.7 36.5 1.0 O A:HOH415 4.8 52.2 1.0 CG A:TYR185 4.9 40.2 1.0

Chlorine binding site 2 out of 2 in the Full Length Structure of Lpmip with Bound Inhibitor JK095


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Full Length Structure of Lpmip with Bound Inhibitor JK095 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:81.2 occ:1.00 CL2 A:9QN301 0.0 81.2 1.0 CAR A:9QN301 1.7 55.7 1.0 CAQ A:9QN301 2.7 54.6 1.0 CAS A:9QN301 2.7 52.7 1.0 CG A:ASP142 3.7 50.1 1.0 OD1 A:ASP142 3.8 58.1 1.0 OD2 A:ASP142 3.9 46.5 1.0 CAP A:9QN301 4.0 55.8 1.0 CAN A:9QN301 4.0 50.2 1.0 CB A:ASP142 4.1 42.7 1.0 O A:PHE141 4.3 45.0 1.0 CAW A:9QN301 4.4 50.4 1.0 CAO A:9QN301 4.5 48.3 1.0 OAX A:9QN301 4.7 54.4 1.0 ZN A:ZN303 4.8 81.7 1.0

C.Wiedemann, J.J.Whittaker, V.H.P.Carrillo, B.Goretzki, M.Dajka, F.Tebbe, J.M.Harder, P.R.Krajczy, B.Joseph, F.Hausch, A.Guskov, U.A.Hellmich. Legionella Pneumophila Macrophage Infectivity Potentiator Protein Appendage Domains Modulate Protein Dynamics and Inhibitor Binding. Int.J.Biol.Macromol. 26366 2023.
ISSN: ISSN 0141-8130
PubMed: 37633566
DOI: 10.1016/J.IJBIOMAC.2023.126366