Sodium in PDB 7c6o: Catalytic Subunit of Cobaltochelatase From Mycobacterium Tuberculosis

All present enzymatic activity of Catalytic Subunit of Cobaltochelatase From Mycobacterium Tuberculosis:
6.6.1.2;

The structure of Catalytic Subunit of Cobaltochelatase From Mycobacterium Tuberculosis, PDB code: 7c6o was solved by J.Zhang, L.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.50 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	65.564, 125.473, 78.551, 90.00, 103.23, 90.00
R / Rfree (%)	16.3 / 19.6

The binding sites of Sodium atom in the Catalytic Subunit of Cobaltochelatase From Mycobacterium Tuberculosis (pdb code 7c6o). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Catalytic Subunit of Cobaltochelatase From Mycobacterium Tuberculosis, PDB code: 7c6o:

Sodium binding site 1 out of 1 in the Catalytic Subunit of Cobaltochelatase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Catalytic Subunit of Cobaltochelatase From Mycobacterium Tuberculosis within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1205 b:22.5 occ:1.00 O A:SER91 2.3 17.6 1.0 O A:ASP89 2.4 18.0 1.0 O A:HOH1802 2.4 27.1 1.0 O A:HOH2062 2.5 34.1 1.0 O A:HOH2060 2.5 31.5 1.0 O A:HOH1654 2.6 17.0 1.0 C A:ASP89 3.5 16.9 1.0 C A:SER91 3.5 14.8 1.0 O A:HOH2025 4.0 32.1 1.0 O A:VAL93 4.0 21.9 1.0 N A:SER91 4.1 16.0 1.0 C A:ARG90 4.1 19.4 1.0 CA A:ASP89 4.2 17.8 1.0 O A:THR88 4.3 13.6 1.0 O A:HOH2075 4.4 50.8 1.0 N A:ARG90 4.4 16.4 1.0 CA A:SER91 4.4 13.2 1.0 O A:HOH2131 4.4 46.7 1.0 O A:ARG90 4.4 17.7 1.0 N A:THR92 4.5 14.6 1.0 CA A:ARG90 4.5 18.8 1.0 CA A:THR92 4.6 16.4 1.0 CB A:SER91 5.0 12.7 1.0

J.H.Zhang, H.Yuan, X.Wang, H.E.Dai, M.Zhang, L.Liu. Crystal Structure of the Large Subunit of Cobaltochelatase From Mycobacterium Tuberculosis. Proteins 2020.
ISSN: ESSN 1097-0134
PubMed: 33210347
DOI: 10.1002/PROT.26023