Zinc in PDB 2yb5: Structure of the Fusidic Acid Resistance Protein Fusc

The structure of Structure of the Fusidic Acid Resistance Protein Fusc, PDB code: 2yb5 was solved by G.Cox, T.A.Edwards, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	34.150, 109.610, 61.150, 90.00, 101.72, 90.00
R / Rfree (%)	21.334 / 28.773

The binding sites of Zinc atom in the Structure of the Fusidic Acid Resistance Protein Fusc (pdb code 2yb5). 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 the Fusidic Acid Resistance Protein Fusc, PDB code: 2yb5:
Jump to Zinc binding site number: 1; 2;

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Fusidic Acid Resistance Protein Fusc within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1213 b:30.9 occ:1.00 SG A:CYS188 2.1 34.1 1.0 SG A:CYS155 2.3 36.3 1.0 SG A:CYS158 2.4 40.3 1.0 SG A:CYS194 2.4 31.2 1.0 CB A:CYS155 3.0 40.1 1.0 CB A:CYS194 3.2 34.2 1.0 CB A:CYS188 3.3 35.0 1.0 CB A:CYS158 3.3 41.5 1.0 CA A:CYS194 3.6 35.4 1.0 N A:CYS158 3.7 40.1 1.0 N A:CYS188 4.0 34.8 1.0 CA A:CYS158 4.2 41.2 1.0 CA A:CYS188 4.2 35.0 1.0 CA A:CYS155 4.5 40.6 1.0 C A:CYS194 4.5 35.5 1.0 CB A:ILE157 4.5 37.2 1.0 O A:CYS194 4.6 35.1 1.0 N A:CYS194 4.6 36.5 1.0 ND2 A:ASN197 4.7 43.0 1.0 C A:ILE157 4.8 39.4 1.0 OG A:SER162 4.9 49.0 1.0 N A:ILE157 4.9 38.4 1.0 C A:CYS155 5.0 40.0 1.0 CG2 A:ILE157 5.0 36.6 1.0 C A:CYS158 5.0 43.0 1.0

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


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Fusidic Acid Resistance Protein Fusc within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn1220 b:27.9 occ:1.00 SG F:CYS158 2.3 34.4 1.0 SG F:CYS194 2.3 28.4 1.0 SG F:CYS188 2.3 36.2 1.0 SG F:CYS155 2.4 34.0 1.0 CB F:CYS194 3.1 29.4 1.0 CB F:CYS155 3.1 38.4 1.0 CB F:CYS158 3.3 35.6 1.0 CB F:CYS188 3.3 35.7 1.0 CA F:CYS194 3.5 30.7 1.0 N F:CYS158 3.7 34.6 1.0 N F:CYS188 4.0 35.3 1.0 CA F:CYS158 4.1 35.7 1.0 CA F:CYS188 4.3 36.3 1.0 C F:CYS194 4.5 29.8 1.0 N F:CYS194 4.6 32.0 1.0 CA F:CYS155 4.6 39.0 1.0 CB F:ILE157 4.6 31.5 1.0 O F:CYS194 4.6 28.3 1.0 C F:ILE157 4.7 33.6 1.0 OG F:SER162 4.8 47.9 1.0 C F:CYS158 4.9 38.1 1.0 OH F:TYR117 4.9 27.2 1.0 C F:CYS155 5.0 37.9 1.0 N F:ILE157 5.0 33.9 1.0

G.Cox, G.S.Thompson, H.T.Jenkins, S.W.Homans, T.A.Edwards, A.J.Oneill. Ribosome Clearance By Fusb-Type Proteins Mediates Resistance to the Antibiotic Fusidic Acid Proc.Natl.Acad.Sci.Usa V. 109 2102 2012.
ISSN: ISSN 0027-8424
PubMed: 22308410
DOI: 10.1073/PNAS.1117275109