Zinc in PDB 4adn: Fusidic Acid Resistance Protein Fusb

The structure of Fusidic Acid Resistance Protein Fusb, PDB code: 4adn was solved by X.Guo, K.Peisker, K.Backbro, Y.Chen, R.K.Kiran, S.Sanyal, M.Selmer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.774 / 1.65
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	75.020, 122.410, 52.920, 90.00, 90.00, 90.00
R / Rfree (%)	16.31 / 20.21

The structure of Fusidic Acid Resistance Protein Fusb also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Sodium	(Na)	8 atoms

The binding sites of Zinc atom in the Fusidic Acid Resistance Protein Fusb (pdb code 4adn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Fusidic Acid Resistance Protein Fusb, PDB code: 4adn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Fusidic Acid Resistance Protein Fusb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Fusidic Acid Resistance Protein Fusb within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1223 b:15.4 occ:1.00 SG A:CYS204 2.3 14.8 1.0 SG A:CYS198 2.3 16.5 1.0 SG A:CYS169 2.3 16.5 1.0 SG A:CYS166 2.4 13.8 1.0 CB A:CYS166 3.1 14.8 1.0 CB A:CYS204 3.2 14.6 1.0 CB A:CYS169 3.3 19.5 1.0 CB A:CYS198 3.3 16.3 1.0 CA A:CYS204 3.6 14.4 1.0 N A:CYS169 3.7 16.7 1.0 N A:CYS198 3.9 14.2 1.0 CA A:CYS169 4.1 18.1 1.0 CA A:CYS198 4.2 13.8 1.0 OE1 A:GLN207 4.2 25.3 1.0 O A:CYS204 4.4 17.1 1.0 C A:CYS204 4.4 15.9 1.0 CB A:ILE168 4.5 13.4 1.0 CA A:CYS166 4.5 14.1 1.0 N A:CYS204 4.7 16.6 1.0 O A:HOH2179 4.8 17.4 1.0 C A:ILE168 4.8 15.3 1.0 OG A:SER173 4.9 22.0 1.0 C A:CYS169 5.0 17.1 1.0

Zinc binding site 2 out of 2 in the Fusidic Acid Resistance Protein Fusb


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Fusidic Acid Resistance Protein Fusb within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1223 b:14.4 occ:1.00 SG B:CYS198 2.3 14.5 1.0 SG B:CYS204 2.3 14.2 1.0 SG B:CYS169 2.4 13.8 1.0 SG B:CYS166 2.4 13.8 1.0 CB B:CYS166 3.1 13.3 1.0 CB B:CYS204 3.2 13.5 1.0 CB B:CYS198 3.2 13.7 1.0 CB B:CYS169 3.3 14.8 1.0 CA B:CYS204 3.6 12.1 1.0 N B:CYS169 3.7 16.0 1.0 N B:CYS198 3.9 13.9 1.0 CA B:CYS169 4.1 14.3 1.0 CA B:CYS198 4.2 13.1 1.0 OE1 B:GLN207 4.3 20.6 1.0 O B:CYS204 4.4 13.1 1.0 C B:CYS204 4.4 11.8 1.0 CB B:ILE168 4.5 15.6 1.0 CA B:CYS166 4.6 12.6 1.0 N B:CYS204 4.7 14.1 1.0 C B:ILE168 4.8 16.4 1.0 O B:HOH2145 4.8 17.9 1.0 OG B:SER173 4.9 20.2 1.0 CA B:ILE168 5.0 14.7 1.0 C B:CYS169 5.0 14.9 1.0 CG2 B:ILE168 5.0 19.2 1.0 N B:ILE168 5.0 15.2 1.0

X.Guo, K.Peisker, K.Backbro, Y.Chen, R.K.Kiran, C.S.Mandava, S.Sanyal, M.Selmer. Structure and Function of Fusb: An Elongation Factor G-Binding Fusidic Acid Resistance Protein Active in Ribosomal Translocation and Recycling Open Biol. V. 2 20016 2012.
ISSN: ISSN 2046-2441
PubMed: 22645663
DOI: 10.1098/RSOB.120016