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

The structure of Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - Wt, PDB code: 5wba 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)	54.87 / 1.50
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	57.510, 57.510, 183.130, 90.00, 90.00, 90.00
R / Rfree (%)	14 / 15.1

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

Copper binding site 1 out of 2 in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - Wt


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 - Wt within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:37.8 occ:1.00 CU1 A:SI8201 0.0 37.8 1.0 O3 A:SI8201 1.9 40.5 1.0 N6 A:SI8201 2.0 39.9 1.0 N5 A:SI8201 2.0 40.2 1.0 N4 A:SI8201 2.0 30.1 1.0 C20 A:SI8201 2.5 33.4 1.0 C12 A:SI8201 2.8 26.8 1.0 C23 A:SI8201 3.0 42.5 1.0 C22 A:SI8201 3.0 37.1 1.0 C16 A:SI8201 3.0 44.1 1.0 C15 A:SI8201 3.0 36.7 1.0 C13 A:SI8201 3.1 34.7 1.0 C14 A:SI8201 3.2 37.3 1.0 C21 A:SI8201 3.2 35.6 1.0 O4 A:SI8201 3.3 42.1 1.0 O A:HOH322 4.2 23.3 0.7 C11 A:SI8201 4.3 20.8 1.0 C24 A:SI8201 4.3 42.4 1.0 C26 A:SI8201 4.3 38.5 1.0 C17 A:SI8201 4.3 45.1 1.0 C19 A:SI8201 4.3 39.9 1.0 C25 A:SI8201 4.8 41.1 1.0 C18 A:SI8201 4.8 40.9 1.0

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


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 - Wt within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu204 b:55.1 occ:0.50 NE2 A:HIS87 2.3 16.7 1.0 CD2 A:HIS87 3.3 16.3 1.0 CE1 A:HIS87 3.3 16.2 1.0 O A:HOH307 3.9 34.5 1.0 ND1 A:HIS87 4.4 15.6 1.0 CG A:HIS87 4.4 15.4 1.0 O A:ASN85 4.7 14.8 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