Chlorine in PDB 3oxh: Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577

The structure of Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577, PDB code: 3oxh was solved by N.Echols, E.M.Flynn, S.Stephenson, H.-L.Ng, T.Alber, Tb Structuralgenomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.75
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.597, 81.981, 36.037, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21.2

The structure of Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577 also contains other interesting chemical elements:

Mercury

(Hg)

1 atom

The binding sites of Chlorine atom in the Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577 (pdb code 3oxh). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577, PDB code: 3oxh:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:32.5 occ:1.00 O A:HOH410 2.7 31.5 1.0 O A:HOH397 2.8 33.6 1.0 N A:VAL228 3.0 14.7 1.0 CA A:GLN227 3.7 17.5 1.0 CB A:VAL228 3.8 13.5 1.0 CG A:GLN227 3.8 21.6 1.0 C A:GLN227 3.8 15.1 1.0 CA A:VAL228 3.9 13.4 1.0 CG2 A:VAL228 4.0 14.8 1.0 CB A:ALA222 4.0 16.5 1.0 O A:VAL228 4.2 14.6 1.0 CB A:GLN227 4.3 17.9 1.0 C A:VAL228 4.5 13.6 1.0 O A:GLY226 4.7 15.7 1.0 CA A:ALA222 4.8 16.1 1.0 N A:GLN227 4.9 15.6 1.0 CD A:GLN227 5.0 23.4 1.0

Chlorine binding site 2 out of 2 in the Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Mycobacterium Tuberculosis Kinase Inhibitor Homolog RV0577 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:34.7 occ:1.00 O A:HOH371 3.1 34.1 1.0 CA A:ALA24 3.5 24.7 1.0 CB A:ALA24 3.6 25.6 1.0 N A:ALA24 3.8 25.9 1.0 CE A:LYS27 3.8 30.1 1.0 CD A:LYS27 3.9 27.6 1.0 C A:SER23 4.1 26.4 1.0 O A:SER23 4.3 26.3 1.0 CB A:SER23 4.4 29.9 1.0 CG A:LYS27 4.8 25.7 1.0 OD1 A:ASP21 4.8 27.1 1.0 C A:ALA24 4.9 22.7 1.0 CA A:SER23 4.9 28.0 1.0

G.W.Buchko, N.Echols, E.M.Flynn, H.L.Ng, S.Stephenson, H.B.Kim, P.J.Myler, T.C.Terwilliger, T.Alber, C.Y.Kim. Structural and Biophysical Characterization of the Mycobacterium Tuberculosis Protein RV0577, A Protein Associated with Neutral Red Staining of Virulent Tuberculosis Strains and Homologue of the Streptomyces Coelicolor Protein Kbpa. Biochemistry 2017.
ISSN: ISSN 1520-4995
PubMed: 28692281
DOI: 10.1021/ACS.BIOCHEM.7B00511