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Gold in PDB 7ff0: Pseudomonas Aeruginosa Virulence Factor Regulator with Camp Ligand and Auranofin

Protein crystallography data

The structure of Pseudomonas Aeruginosa Virulence Factor Regulator with Camp Ligand and Auranofin, PDB code: 7ff0 was solved by B.L.A.Chew, D.Luo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.12 / 2.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 135.6, 49.643, 63.915, 90, 100.37, 90
R / Rfree (%) 20.7 / 23.9

Gold Binding Sites:

The binding sites of Gold atom in the Pseudomonas Aeruginosa Virulence Factor Regulator with Camp Ligand and Auranofin (pdb code 7ff0). This binding sites where shown within 5.0 Angstroms radius around Gold atom.
In total only one binding site of Gold was determined in the Pseudomonas Aeruginosa Virulence Factor Regulator with Camp Ligand and Auranofin, PDB code: 7ff0:

Gold binding site 1 out of 1 in 7ff0

Go back to Gold Binding Sites List in 7ff0
Gold binding site 1 out of 1 in the Pseudomonas Aeruginosa Virulence Factor Regulator with Camp Ligand and Auranofin


Mono view


Stereo pair view

A full contact list of Gold with other atoms in the Au binding site number 1 of Pseudomonas Aeruginosa Virulence Factor Regulator with Camp Ligand and Auranofin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Au305

b:88.5
occ:1.00
SG A:CYS183 2.7 61.4 1.0
HA A:CYS183 3.3 34.7 1.0
HG21 A:VAL144 3.5 30.4 1.0
HB2 A:CYS183 3.6 36.8 1.0
CB A:CYS183 3.6 39.6 1.0
O A:GLY182 3.9 40.5 1.0
CA A:CYS183 3.9 38.9 1.0
H A:SER184 4.2 40.6 1.0
CG2 A:VAL144 4.3 32.4 1.0
HG22 A:VAL144 4.3 30.4 1.0
HD2 B:PHE141 4.4 45.7 1.0
HG23 A:VAL144 4.5 30.4 1.0
HB3 A:CYS183 4.5 36.8 1.0
HA B:PHE141 4.7 40.7 1.0
SD A:MET187 4.7 71.2 1.0
C A:GLY182 4.8 38.2 1.0
N A:SER184 4.9 42.8 1.0
N A:CYS183 4.9 38.7 1.0

Reference:

B.L.A.Chew, D.Luo, L.Yang. Inhibitory Mechanism of Gold Analogues Against Pseudomonas Global Virulence Factor Regulator Vfr To Be Published.
Page generated: Tue Apr 4 17:16:53 2023

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