Zinc in PDB 8hfm: Crystal Structure of Mycobacterium Smegmatis Mshc

All present enzymatic activity of Crystal Structure of Mycobacterium Smegmatis Mshc:
6.3.1.13;

The structure of Crystal Structure of Mycobacterium Smegmatis Mshc, PDB code: 8hfm was solved by L.Pang, S.D.Weeks, S.V.Strelkov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.32 / 2.41
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	69.81, 69.81, 236.011, 90, 90, 90
R / Rfree (%)	20.6 / 23.8

The structure of Crystal Structure of Mycobacterium Smegmatis Mshc also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Mycobacterium Smegmatis Mshc (pdb code 8hfm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Mycobacterium Smegmatis Mshc, PDB code: 8hfm:

Zinc binding site 1 out of 1 in the Crystal Structure of Mycobacterium Smegmatis Mshc


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 Smegmatis Mshc within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:54.6 occ:1.00 NE2 A:HIS256 2.2 53.1 1.0 O A:HOH661 2.3 37.1 1.0 SG A:CYS231 2.3 55.5 1.0 SG A:CYS43 2.3 53.3 1.0 CD2 A:HIS256 3.0 51.8 1.0 CB A:CYS43 3.1 48.6 1.0 CE1 A:HIS256 3.4 56.2 1.0 CB A:CYS231 3.4 49.0 1.0 CA A:CYS43 4.0 51.7 1.0 CG A:HIS256 4.2 52.4 1.0 NE1 A:TRP227 4.2 58.0 1.0 CE2 A:TYR41 4.3 54.5 1.0 ND1 A:HIS256 4.4 56.6 1.0 ND2 A:ASN81 4.4 57.4 1.0 OH A:TYR41 4.5 57.3 1.0 OD1 A:ASN81 4.5 62.7 1.0 NE2 A:HIS257 4.7 45.7 1.0 CG A:ASN81 4.8 61.3 1.0 CA A:CYS231 4.8 58.8 1.0 CE2 A:TRP227 4.8 57.9 1.0 CZ A:TYR41 4.9 54.1 1.0 CD2 A:HIS257 4.9 45.8 1.0 CZ2 A:TRP227 5.0 53.9 1.0 N A:CYS43 5.0 53.7 1.0

L.Pang, S.Lenders, E.M.Osipov, S.D.Weeks, J.Rozenski, T.Piller, D.Cappoen, S.V.Strelkov, A.Van Aerschot. Structural Basis of Cysteine Ligase Mshc Inhibition By Cysteinyl-Sulfonamides. Int J Mol Sci V. 23 2022.
ISSN: ESSN 1422-0067
PubMed: 36499418
DOI: 10.3390/IJMS232315095