Copper in PDB 3sb6: Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization

All present enzymatic activity of Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization:
3.2.1.17;

The structure of Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization, PDB code: 3sb6 was solved by A.B.Soriaga, A.Laganowsky, M.Zhao, M.R.Sawaya, D.Cascio, T.O.Yeates, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.040, 69.840, 89.040, 90.00, 90.00, 90.00
R / Rfree (%)	22.6 / 27.2

The structure of Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Copper atom in the Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization (pdb code 3sb6). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization, PDB code: 3sb6:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu163 b:47.5 occ:1.00 NE2 A:HIS76 2.0 46.7 1.0 OD2 A:ASP72 2.2 61.1 1.0 NE2 B:HIS65 2.2 45.7 1.0 NE2 B:HIS61 2.2 45.0 1.0 OD1 A:ASP72 2.8 53.5 1.0 CG A:ASP72 2.8 52.2 1.0 CD2 B:HIS61 2.9 44.1 1.0 CE1 A:HIS76 3.0 47.8 1.0 CD2 A:HIS76 3.1 45.2 1.0 CD2 B:HIS65 3.2 44.5 1.0 CE1 B:HIS65 3.2 45.9 1.0 CE1 B:HIS61 3.4 44.6 1.0 CG B:HIS61 4.1 41.5 1.0 ND1 A:HIS76 4.2 47.7 1.0 CG A:HIS76 4.2 44.0 1.0 CG B:HIS65 4.3 42.6 1.0 ND1 B:HIS65 4.3 45.6 1.0 CB A:ASP72 4.3 37.9 1.0 ND1 B:HIS61 4.4 43.9 1.0 O A:HOH167 4.9 53.2 1.0

Copper binding site 2 out of 2 in the Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu-Mediated Dimer of T4 Lysozyme D61H/K65H/R76H/R80H By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu163 b:59.0 occ:1.00 NE2 B:HIS76 2.0 65.6 1.0 NE2 A:HIS65 2.3 50.3 1.0 NE2 A:HIS61 2.3 52.1 1.0 OD1 B:ASP72 2.5 62.8 1.0 OD2 B:ASP72 2.6 67.0 1.0 CG B:ASP72 2.9 61.0 1.0 CD2 A:HIS61 2.9 50.8 1.0 CD2 B:HIS76 3.0 64.8 1.0 CE1 B:HIS76 3.0 66.6 1.0 CD2 A:HIS65 3.1 48.2 1.0 CE1 A:HIS65 3.2 50.7 1.0 CE1 A:HIS61 3.6 51.5 1.0 CG B:HIS76 4.1 63.7 1.0 CG A:HIS65 4.1 45.9 1.0 ND1 B:HIS76 4.2 67.1 1.0 CG A:HIS61 4.2 47.8 1.0 ND1 A:HIS65 4.2 49.6 1.0 CB B:ASP72 4.4 49.6 1.0 ND1 A:HIS61 4.5 50.4 1.0 O B:ASP72 4.9 53.4 1.0

A.Laganowsky, M.Zhao, A.B.Soriaga, M.R.Sawaya, D.Cascio, T.O.Yeates. An Approach to Crystallizing Proteins By Metal-Mediated Synthetic Symmetrization. Protein Sci. V. 20 1876 2011.
ISSN: ISSN 0961-8368
PubMed: 21898649
DOI: 10.1002/PRO.727