Copper in PDB 5wbd: Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - N49A

The structure of Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - N49A, PDB code: 5wbd 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)	54.63 / 1.50
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	57.510, 57.510, 174.810, 90.00, 90.00, 90.00
R / Rfree (%)	15.4 / 17.8

The binding sites of Copper atom in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - N49A (pdb code 5wbd). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - N49A, PDB code: 5wbd:

Copper binding site 1 out of 1 in the Peroxide Activation Regulated By Hydrogen Bonds Within Artificial Cu Proteins - N49A


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 - N49A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:23.9 occ:1.00 CU1 A:SI7201 0.0 23.9 1.0 N5 A:SI7201 2.0 25.6 1.0 N6 A:SI7201 2.0 27.3 1.0 N4 A:SI7201 2.0 21.8 1.0 O3 A:SI7201 2.5 26.3 1.0 C12 A:SI7201 2.7 20.6 1.0 C20 A:SI7201 2.9 23.5 1.0 C16 A:SI7201 2.9 26.1 1.0 C22 A:SI7201 3.0 23.6 1.0 C13 A:SI7201 3.0 26.2 1.0 C23 A:SI7201 3.0 31.4 1.0 C15 A:SI7201 3.0 24.6 1.0 C21 A:SI7201 3.1 23.6 1.0 C14 A:SI7201 3.4 27.6 1.0 C11 A:SI7201 4.2 17.3 1.0 C17 A:SI7201 4.2 25.1 1.0 O A:HOH331 4.3 17.1 0.7 C26 A:SI7201 4.3 26.3 1.0 C24 A:SI7201 4.3 32.0 1.0 C19 A:SI7201 4.3 23.8 1.0 C18 A:SI7201 4.8 23.0 1.0 C25 A:SI7201 4.8 30.7 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