Zinc in PDB 8f5v: Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+

The structure of Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+, PDB code: 8f5v was solved by Y.P.Jayasinghe, D.R.Ronning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.70 / 1.45
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	75.027, 76.732, 53.261, 90, 90, 90
R / Rfree (%)	17.9 / 20.3

The binding sites of Zinc atom in the Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+ (pdb code 8f5v). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+, PDB code: 8f5v:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn202 b:13.8 occ:1.00 OD2 A:ASP155 2.1 13.9 1.0 NE2 A:HIS52 2.1 9.4 1.0 NE2 A:HIS159 2.2 13.8 1.0 O32 A:XGZ201 2.2 17.2 0.9 S31 A:XGZ201 2.3 19.6 0.7 CG A:ASP155 2.9 17.4 1.0 OD1 A:ASP155 3.0 20.6 1.0 C24 A:XGZ201 3.0 20.2 1.0 CD2 A:HIS159 3.0 11.4 1.0 C30 A:XGZ201 3.0 23.6 0.4 CE1 A:HIS52 3.1 12.6 1.0 CD2 A:HIS52 3.1 10.7 1.0 N26 A:XGZ201 3.1 18.3 0.7 C25 A:XGZ201 3.2 25.3 1.0 CE1 A:HIS159 3.2 12.7 1.0 C27 A:XGZ201 4.1 20.5 0.8 ND1 A:HIS52 4.2 12.8 1.0 CG A:HIS159 4.2 11.4 1.0 CG A:HIS52 4.2 11.8 1.0 ND1 A:HIS159 4.3 12.8 1.0 CB A:ASP155 4.3 13.8 1.0 N23 A:XGZ201 4.4 17.8 1.0 C28 A:XGZ201 4.7 20.1 1.0 CG2 A:VAL56 4.7 16.2 1.0 O29 A:XGZ201 4.8 20.4 0.6 C22 A:XGZ201 4.9 15.7 0.8

Zinc binding site 2 out of 4 in the Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn203 b:16.2 occ:1.00 NE2 A:HIS87 2.1 14.2 1.0 O A:HOH453 2.2 14.5 1.0 CD2 A:HIS87 3.0 17.9 1.0 CE1 A:HIS87 3.2 18.5 1.0 CG A:HIS87 4.2 17.4 1.0 ND1 A:HIS87 4.2 18.5 1.0 CD A:ARG86 4.9 24.0 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn202 b:16.6 occ:0.89 OD2 B:ASP155 2.1 20.1 1.0 NE2 B:HIS52 2.2 15.9 1.0 NE2 B:HIS159 2.2 17.0 1.0 O32 B:XGZ201 2.2 24.7 0.8 S31 B:XGZ201 2.3 28.8 0.8 CG B:ASP155 2.9 22.1 1.0 CD2 B:HIS159 2.9 13.1 1.0 OD1 B:ASP155 3.0 22.4 1.0 C24 B:XGZ201 3.0 25.7 0.8 N26 B:XGZ201 3.1 25.4 0.8 CD2 B:HIS52 3.1 16.9 1.0 CE1 B:HIS52 3.1 15.6 1.0 C25 B:XGZ201 3.3 26.9 0.8 CE1 B:HIS159 3.3 16.9 1.0 C30 B:XGZ201 3.3 31.0 0.8 C27 B:XGZ201 4.0 21.7 0.8 CG B:HIS159 4.2 13.0 1.0 ND1 B:HIS52 4.2 18.4 1.0 CG B:HIS52 4.3 15.2 1.0 ND1 B:HIS159 4.3 14.0 1.0 CB B:ASP155 4.3 16.7 1.0 N23 B:XGZ201 4.4 22.2 0.8 C28 B:XGZ201 4.6 22.6 0.8 CG2 B:VAL56 4.7 18.4 1.0 O29 B:XGZ201 4.7 26.9 0.8 C22 B:XGZ201 5.0 22.0 0.8

Zinc binding site 4 out of 4 in the Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Mycobacterium Tuberculosis Mycothiol S- Transferase Enzyme in Complex with Mycothiol and ZN2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn203 b:24.1 occ:1.00 ND1 B:HIS87 2.3 27.9 1.0 O B:HOH410 2.5 17.1 1.0 CE1 B:HIS87 2.5 20.0 1.0 CG B:HIS87 3.7 20.1 1.0 NE2 B:HIS87 3.8 30.4 1.0 O B:HOH453 4.3 37.6 1.0 CD2 B:HIS87 4.4 24.0 1.0 CB B:ARG86 4.4 24.2 1.0 CD B:ARG86 4.5 25.7 1.0 CB B:HIS87 4.6 23.0 1.0 CG B:ARG86 4.7 21.5 1.0

Y.P.Jayasinghe, M.T.Banco, J.J.Lindenberger, L.Favrot, Z.Palcekova, M.Jackson, S.Manabe, D.R.Ronning. The Mycobacterium Tuberculosis Mycothiol S -Transferase Is Divalent Metal-Dependent For Mycothiol Binding and Transfer. Rsc Med Chem V. 14 491 2023.
ISSN: ESSN 2632-8682
PubMed: 36970142
DOI: 10.1039/D2MD00401A