Mercury in PDB 6njx: C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury

The structure of C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury, PDB code: 6njx was solved by C.J.Schiltz, A.Lee, E.A.Partlow, C.J.Hosford, J.S.Chappie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.10 / 1.95
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	65.189, 65.189, 63.799, 90.00, 90.00, 90.00
R / Rfree (%)	20.1 / 24.2

The structure of C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury also contains other interesting chemical elements:

Iodine

(I)

3 atoms

The binding sites of Mercury atom in the C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury (pdb code 6njx). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury, PDB code: 6njx:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in the C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg701 b:44.5 occ:0.20 O A:HOH880 2.3 54.8 1.0 HG A:HG702 2.6 38.1 0.2 N A:ILE390 2.9 62.0 1.0 O A:HOH879 2.9 69.1 1.0 CB A:CYS427 3.1 44.8 0.5 CB A:CYS427 3.1 45.2 0.5 SG A:CYS427 3.3 56.7 0.5 SG A:CYS427 3.3 56.7 0.5 HG A:HG703 3.4 75.3 0.2 CA A:ILE390 3.6 76.4 1.0 O A:HOH878 4.1 56.3 1.0 O A:ILE390 4.1 77.3 1.0 OG1 A:THR425 4.3 53.5 1.0 CG1 A:VAL396 4.4 34.5 1.0 C A:ILE390 4.4 80.4 1.0 CA A:CYS427 4.5 42.7 0.5 CA A:CYS427 4.5 42.6 0.5 CG2 A:VAL396 4.8 36.8 1.0 CG1 A:ILE390 4.8 81.5 1.0 CB A:ILE390 4.8 80.2 1.0

Mercury binding site 2 out of 3 in the C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg702 b:38.1 occ:0.24 O A:HOH880 2.4 54.8 1.0 HG A:HG701 2.6 44.5 0.2 SG A:CYS427 3.9 56.7 0.5 SG A:CYS427 3.9 56.7 0.5 CD2 A:TYR437 3.9 45.2 1.0 O A:ILE390 4.1 77.3 1.0 O A:HOH878 4.1 56.3 1.0 CD2 A:LEU440 4.2 45.2 1.0 CG1 A:VAL396 4.3 34.5 1.0 CD1 A:LEU441 4.3 35.0 1.0 CE2 A:TYR437 4.3 49.6 1.0 CB A:CYS427 4.4 44.8 0.5 CB A:CYS427 4.4 45.2 0.5 CD2 A:LEU441 4.4 41.5 1.0 CG2 A:VAL396 4.5 36.8 1.0 N A:ILE390 4.6 62.0 1.0 CD2 A:LEU398 4.7 38.2 1.0 CG A:LEU441 4.7 40.5 1.0 O A:HOH879 4.7 69.1 1.0 CA A:ILE390 4.9 76.4 1.0 C A:ILE390 5.0 80.4 1.0 CB A:VAL396 5.0 34.5 1.0

Mercury binding site 3 out of 3 in the C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 3 of C-Terminal Region of the Xanthomonas Campestris Pv. Campestris Old Protein Phased with Mercury within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg703 b:75.3 occ:0.24 O A:HOH879 2.3 69.1 1.0 O A:HOH877 2.9 65.3 1.0 HG A:HG701 3.4 44.5 0.2 CB A:CYS427 3.7 45.2 0.5 CB A:CYS427 3.7 44.8 0.5 O A:VAL426 3.8 46.8 1.0 CA A:CYS427 3.8 42.7 0.5 CA A:CYS427 3.8 42.6 0.5 SG A:CYS427 4.1 56.7 0.5 SG A:CYS427 4.2 56.7 0.5 CG1 A:ILE390 4.4 81.5 1.0 O A:HOH880 4.4 54.8 1.0 C A:VAL426 4.4 44.0 1.0 N A:CYS427 4.5 40.4 1.0 N A:ILE390 4.6 62.0 1.0

C.J.Schiltz, A.Lee, E.A.Partlow, C.J.Hosford, J.S.Chappie. Structural Characterization of Class 2 Old Family Nucleases Supports A Two-Metal Catalysis Mechanism For Cleavage. Nucleic Acids Res. V. 47 9448 2019.
ISSN: ESSN 1362-4962
PubMed: 31400118
DOI: 10.1093/NAR/GKZ703