Chlorine in PDB 8bje: A Structure of the Truncated Lpmip with Bound Inhibitor JK236.

All present enzymatic activity of A Structure of the Truncated Lpmip with Bound Inhibitor JK236.:
5.2.1.8;

The structure of A Structure of the Truncated Lpmip with Bound Inhibitor JK236., PDB code: 8bje 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)	45.86 / 1.49
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	52.951, 52.951, 73.146, 90, 90, 120
R / Rfree (%)	19.8 / 23.3

The binding sites of Chlorine atom in the A Structure of the Truncated Lpmip with Bound Inhibitor JK236. (pdb code 8bje). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the A Structure of the Truncated Lpmip with Bound Inhibitor JK236., PDB code: 8bje:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the A Structure of the Truncated Lpmip with Bound Inhibitor JK236.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of A Structure of the Truncated Lpmip with Bound Inhibitor JK236. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:28.9 occ:1.00 CL1 A:WRL203 0.0 28.9 1.0 C1 A:WRL203 1.7 26.9 1.0 C2 A:WRL203 2.7 25.1 1.0 C22 A:WRL203 2.7 26.6 1.0 OD2 A:ASP65 3.7 25.2 1.0 CG A:ASP65 3.7 23.1 1.0 OD1 A:ASP65 4.0 23.0 1.0 C21 A:WRL203 4.0 26.7 1.0 C3 A:WRL203 4.0 24.2 1.0 CB A:ASP65 4.1 22.4 1.0 O A:PHE64 4.4 22.1 1.0 C20 A:WRL203 4.5 25.0 1.0 O A:HOH301 4.8 26.5 1.0

Chlorine binding site 2 out of 2 in the A Structure of the Truncated Lpmip with Bound Inhibitor JK236.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of A Structure of the Truncated Lpmip with Bound Inhibitor JK236. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:28.6 occ:1.00 CL2 A:WRL203 0.0 28.6 1.0 C21 A:WRL203 1.7 26.7 1.0 C20 A:WRL203 2.7 25.0 1.0 C22 A:WRL203 2.7 26.6 1.0 NH1 A:ARG111 3.3 67.4 1.0 C15 A:WRL203 3.7 21.5 1.0 CG1 A:ILE117 3.9 31.2 1.0 C1 A:WRL203 4.0 26.9 1.0 C3 A:WRL203 4.0 24.2 1.0 CZ A:TYR108 4.1 21.1 1.0 OH A:TYR108 4.1 21.1 1.0 CG A:PRO116 4.2 45.2 1.0 N3 A:WRL203 4.2 21.1 1.0 CE2 A:TYR108 4.3 20.5 1.0 CE1 A:TYR108 4.4 21.8 1.0 O A:HOH303 4.4 46.4 1.0 C16 A:WRL203 4.4 21.2 1.0 C2 A:WRL203 4.5 25.1 1.0 CZ A:ARG111 4.5 67.8 1.0 CB A:ILE117 4.7 30.5 1.0 CD2 A:TYR108 4.9 20.5 1.0 CD1 A:TYR108 4.9 22.5 1.0 CD1 A:ILE117 5.0 31.8 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