Copper in PDB 5wbb: Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A

The structure of Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A, PDB code: 5wbb was solved by S.I.Mann, T.Heinisch, T.R.Ward, A.S.Borovik, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.00 / 1.50
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	57.640, 57.640, 183.980, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 18.8

The binding sites of Copper atom in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A (pdb code 5wbb). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A, PDB code: 5wbb:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:29.8 occ:0.70 CU1 A:SQ1201 0.0 29.8 0.7 N6 A:SQ1201 1.2 25.3 0.3 C23 A:SQ1201 1.5 30.0 0.3 CU1 A:SQ1201 1.6 22.5 0.3 N6 A:SQ1201 2.0 31.0 0.7 N5 A:SQ1201 2.0 40.7 0.7 N4 A:SQ1201 2.0 27.0 0.7 C22 A:SQ1201 2.6 26.8 0.3 C20 A:SQ1201 2.8 30.2 0.7 C12 A:SQ1201 2.8 24.6 0.7 C13 A:SQ1201 2.8 29.4 0.7 C24 A:SQ1201 2.9 23.6 0.3 C16 A:SQ1201 2.9 42.1 0.7 C23 A:SQ1201 2.9 30.4 0.7 C22 A:SQ1201 3.0 31.4 0.7 O A:HOH385 3.0 33.2 1.0 C15 A:SQ1201 3.0 41.4 0.7 N5 A:SQ1201 3.2 20.3 0.3 C14 A:SQ1201 3.2 33.8 0.7 N4 A:SQ1201 3.3 21.9 0.3 C21 A:SQ1201 3.3 30.0 0.7 C26 A:SQ1201 3.5 25.4 0.3 C21 A:SQ1201 3.5 26.0 0.3 C16 A:SQ1201 3.6 19.5 0.3 C25 A:SQ1201 3.6 27.8 0.3 C20 A:SQ1201 3.7 23.5 0.3 C11 A:SQ1201 3.8 17.7 0.3 C12 A:SQ1201 3.9 21.0 0.3 O A:HOH304 4.1 20.5 0.3 C11 A:SQ1201 4.2 19.9 0.7 C17 A:SQ1201 4.2 40.1 0.7 C24 A:SQ1201 4.3 29.7 0.7 C26 A:SQ1201 4.3 28.7 0.7 C19 A:SQ1201 4.3 46.6 0.7 C13 A:SQ1201 4.4 21.3 0.3 C15 A:SQ1201 4.4 20.2 0.3 C14 A:SQ1201 4.6 20.4 0.3 C18 A:SQ1201 4.8 44.5 0.7 C25 A:SQ1201 4.8 29.9 0.7 C17 A:SQ1201 5.0 18.9 0.3

Copper binding site 2 out of 3 in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:22.5 occ:0.30 CU1 A:SQ1201 0.0 22.5 0.3 N4 A:SQ1201 0.9 27.0 0.7 C20 A:SQ1201 1.5 30.2 0.7 C13 A:SQ1201 1.6 29.4 0.7 CU1 A:SQ1201 1.6 29.8 0.7 N5 A:SQ1201 2.0 20.3 0.3 N4 A:SQ1201 2.0 21.9 0.3 N6 A:SQ1201 2.0 25.3 0.3 C14 A:SQ1201 2.1 33.8 0.7 C12 A:SQ1201 2.3 24.6 0.7 N5 A:SQ1201 2.5 40.7 0.7 C15 A:SQ1201 2.7 41.4 0.7 C21 A:SQ1201 2.7 30.0 0.7 C12 A:SQ1201 2.8 21.0 0.3 C20 A:SQ1201 2.8 23.5 0.3 C13 A:SQ1201 2.8 21.3 0.3 N6 A:SQ1201 2.9 31.0 0.7 C16 A:SQ1201 2.9 19.5 0.3 C15 A:SQ1201 2.9 20.2 0.3 C23 A:SQ1201 3.0 30.0 0.3 C22 A:SQ1201 3.0 26.8 0.3 C14 A:SQ1201 3.0 20.4 0.3 C22 A:SQ1201 3.2 31.4 0.7 C21 A:SQ1201 3.2 26.0 0.3 C11 A:SQ1201 3.3 17.7 0.3 C11 A:SQ1201 3.5 19.9 0.7 C16 A:SQ1201 3.8 42.1 0.7 O A:HOH304 4.0 20.5 0.3 O A:HOH385 4.1 33.2 1.0 C19 A:SQ1201 4.1 46.6 0.7 C23 A:SQ1201 4.2 30.4 0.7 C17 A:SQ1201 4.2 18.9 0.3 C19 A:SQ1201 4.2 18.3 0.3 C26 A:SQ1201 4.3 25.4 0.3 C24 A:SQ1201 4.3 23.6 0.3 C26 A:SQ1201 4.6 28.7 0.7 N3 A:SQ1201 4.7 15.0 0.3 C18 A:SQ1201 4.7 17.7 0.3 N3 A:SQ1201 4.8 14.4 0.7 C25 A:SQ1201 4.8 27.8 0.3 C17 A:SQ1201 4.9 40.1 0.7

Copper binding site 3 out of 3 in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - S112A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu202 b:77.2 occ:1.00 NE2 A:HIS87 2.4 15.4 1.0 CD2 A:HIS87 3.4 14.8 1.0 CE1 A:HIS87 3.4 15.2 1.0 O A:HOH319 4.2 34.1 1.0 ND1 A:HIS87 4.5 15.6 1.0 CG A:HIS87 4.5 15.5 1.0 O A:ASN85 4.8 15.2 1.0

S.I.Mann, T.Heinisch, T.R.Ward, A.S.Borovik. Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins. J. Am. Chem. Soc. V. 139 17289 2017.
ISSN: ESSN 1520-5126
PubMed: 29117678
DOI: 10.1021/JACS.7B10452