Chlorine in PDB 3hx9: Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site

The structure of Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site, PDB code: 3hx9 was solved by N.Chim, T.Q.Nguyen, A.Iniguez, C.W.Goulding, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.35 / 1.75
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	43.971, 64.622, 71.082, 90.00, 90.01, 90.00
R / Rfree (%)	18.6 / 23.1

The structure of Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Chlorine atom in the Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site (pdb code 3hx9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site, PDB code: 3hx9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:18.2 occ:1.00 FE A:HEM200 2.4 18.2 1.0 OD1 A:ASN7 3.2 22.5 1.0 ND A:HEM200 3.3 17.8 1.0 NA A:HEM200 3.4 20.1 1.0 NC A:HEM200 3.4 19.3 1.0 NB A:HEM200 3.4 19.2 1.0 CG2 A:VAL53 3.6 13.3 1.0 CZ A:PHE23 3.6 16.5 1.0 CB A:ASN7 3.8 12.3 1.0 CG2 A:ILE9 3.9 24.4 1.0 CG A:ASN7 3.9 15.7 1.0 CB A:VAL53 3.9 12.8 1.0 C1A A:HEM200 3.9 19.8 1.0 C4D A:HEM200 4.0 19.9 1.0 C1C A:HEM200 4.0 18.7 1.0 C4C A:HEM200 4.0 17.6 1.0 C4B A:HEM200 4.0 19.5 1.0 C1D A:HEM200 4.1 19.0 1.0 CG1 A:VAL53 4.1 12.5 1.0 C4A A:HEM200 4.2 18.8 1.0 CD1 A:ILE9 4.2 28.2 1.0 CHA A:HEM200 4.2 18.4 1.0 CE1 A:PHE23 4.2 19.7 1.0 C1B A:HEM200 4.2 16.7 1.0 CHC A:HEM200 4.2 16.9 1.0 CHD A:HEM200 4.4 21.8 1.0 CHB A:HEM200 4.6 20.6 1.0 CE2 A:PHE23 4.8 20.9 1.0 C3C A:HEM200 4.8 20.8 1.0 CG1 A:ILE9 4.8 20.4 1.0 C2C A:HEM200 4.9 16.3 1.0 CB A:ILE9 4.9 19.0 1.0 O A:ASN7 4.9 14.4 1.0 C2A A:HEM200 4.9 21.8 1.0 C3D A:HEM200 5.0 19.8 1.0

Chlorine binding site 2 out of 2 in the Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Heme-Degrader, Mhud (RV3592), From Mycobacterium Tuberculosis with Two Hemes Bound in Its Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:18.4 occ:1.00 FE B:HEM200 2.3 18.5 1.0 OD1 B:ASN7 3.2 21.7 1.0 ND B:HEM200 3.3 17.6 1.0 NC B:HEM200 3.4 19.6 1.0 NA B:HEM200 3.4 21.8 1.0 NB B:HEM200 3.4 21.2 1.0 CG2 B:VAL53 3.6 13.4 1.0 CZ B:PHE23 3.7 14.7 1.0 CG2 B:ILE9 3.8 24.9 1.0 CB B:ASN7 3.8 12.5 1.0 C4C B:HEM200 3.9 16.9 1.0 CG B:ASN7 4.0 15.3 1.0 CB B:VAL53 4.0 13.5 1.0 C1C B:HEM200 4.0 18.1 1.0 C1A B:HEM200 4.0 20.8 1.0 C4D B:HEM200 4.0 18.4 1.0 C4B B:HEM200 4.0 20.2 1.0 C1D B:HEM200 4.1 19.3 1.0 CG1 B:VAL53 4.1 12.3 1.0 CE1 B:PHE23 4.2 17.7 1.0 C4A B:HEM200 4.2 21.4 1.0 C1B B:HEM200 4.2 16.7 1.0 CHA B:HEM200 4.2 18.4 1.0 CHC B:HEM200 4.3 17.2 1.0 CHD B:HEM200 4.3 20.3 1.0 CD1 B:ILE9 4.5 27.0 1.0 CHB B:HEM200 4.6 19.8 1.0 CE2 B:PHE23 4.8 19.9 1.0 C3C B:HEM200 4.8 21.1 1.0 C2C B:HEM200 4.8 15.8 1.0 CG1 B:ILE9 4.9 18.9 1.0 CB B:ILE9 4.9 18.8 1.0 O B:ASN7 4.9 13.8 1.0 C2A B:HEM200 5.0 23.4 1.0 C3D B:HEM200 5.0 18.2 1.0

N.Chim, A.Iniguez, T.Q.Nguyen, C.W.Goulding. Unusual Diheme Conformation of the Heme-Degrading Protein From Mycobacterium Tuberculosis J.Mol.Biol. V. 395 595 2009.
ISSN: ISSN 0022-2836
PubMed: 19917297
DOI: 10.1016/J.JMB.2009.11.025