Zinc in PDB 3hcj: Structure of Msrb From Xanthomonas Campestris (Oxidized Form)

All present enzymatic activity of Structure of Msrb From Xanthomonas Campestris (Oxidized Form):
1.8.4.11;

The structure of Structure of Msrb From Xanthomonas Campestris (Oxidized Form), PDB code: 3hcj was solved by F.M.Ranaivoson, B.Kauffmann, F.Favier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.27 / 1.66
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.197, 65.303, 57.957, 90.00, 94.81, 90.00
R / Rfree (%)	20.1 / 24.8

The binding sites of Zinc atom in the Structure of Msrb From Xanthomonas Campestris (Oxidized Form) (pdb code 3hcj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Msrb From Xanthomonas Campestris (Oxidized Form), PDB code: 3hcj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Msrb From Xanthomonas Campestris (Oxidized Form)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Msrb From Xanthomonas Campestris (Oxidized Form) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1000 b:15.1 occ:1.00 SG A:CYS102 2.3 15.3 1.0 SG A:CYS105 2.3 16.2 1.0 SG A:CYS56 2.3 15.4 1.0 SG A:CYS53 2.4 12.9 1.0 CB A:CYS102 3.1 15.3 1.0 CB A:CYS53 3.1 12.4 1.0 CB A:CYS56 3.3 13.1 1.0 CB A:CYS105 3.5 15.6 1.0 N A:CYS105 3.8 15.4 1.0 N A:CYS56 3.8 12.9 1.0 CA A:CYS56 4.1 13.3 1.0 CA A:CYS105 4.2 15.4 1.0 CA A:CYS102 4.5 15.2 1.0 CA A:CYS53 4.6 12.8 1.0 CB A:LEU58 4.7 13.4 1.0 CB A:ARG104 4.7 15.0 1.0 C A:CYS56 4.7 11.7 1.0 CB A:LEU55 4.8 13.1 1.0 C A:ARG104 4.8 15.9 1.0 N A:GLY57 4.9 12.2 1.0 CB A:SER107 4.9 14.3 1.0 C A:CYS105 4.9 16.0 1.0 OG A:SER107 4.9 15.2 1.0 C A:LEU55 4.9 13.3 1.0 N A:LEU58 4.9 12.9 1.0 N A:ASP106 5.0 16.3 1.0

Zinc binding site 2 out of 2 in the Structure of Msrb From Xanthomonas Campestris (Oxidized Form)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Msrb From Xanthomonas Campestris (Oxidized Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1000 b:13.7 occ:1.00 SG B:CYS102 2.3 13.9 1.0 SG B:CYS105 2.3 14.7 1.0 SG B:CYS53 2.4 13.6 1.0 SG B:CYS56 2.4 14.7 1.0 CB B:CYS102 3.1 14.4 1.0 CB B:CYS53 3.1 13.1 1.0 CB B:CYS56 3.3 11.3 1.0 CB B:CYS105 3.4 13.8 1.0 N B:CYS105 3.8 14.4 1.0 N B:CYS56 3.9 12.5 1.0 CA B:CYS56 4.1 12.6 1.0 CA B:CYS105 4.1 13.8 1.0 CA B:CYS53 4.5 12.3 1.0 CA B:CYS102 4.5 13.9 1.0 CB B:SER107 4.7 14.1 1.0 CB B:ARG104 4.7 12.8 1.0 CB B:LEU58 4.7 12.2 1.0 OG B:SER107 4.8 14.7 1.0 C B:CYS56 4.8 12.9 1.0 C B:CYS105 4.8 14.1 1.0 C B:ARG104 4.9 14.4 1.0 CB B:LEU55 4.9 13.0 1.0 N B:GLY57 4.9 12.4 1.0 N B:LEU58 4.9 11.7 1.0 C B:LEU55 5.0 13.5 1.0

F.M.Ranaivoson, F.Neiers, B.Kauffmann, S.Boschi-Muller, G.Branlant, F.Favier. Methionine Sulfoxide Reductase B Displays A High Level of Flexibility. J.Mol.Biol. 2009.
ISSN: ESSN 1089-8638
PubMed: 19733575
DOI: 10.1016/J.JMB.2009.08.073