Copper in PDB 3sb9: Cu-Mediated Dimer of T4 Lysozyme R76H/R80H By Synthetic Symmetrization

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

The structure of Cu-Mediated Dimer of T4 Lysozyme R76H/R80H By Synthetic Symmetrization, PDB code: 3sb9 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)	79.11 / 2.45
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	79.114, 79.114, 87.367, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 23.9

The binding sites of Copper atom in the Cu-Mediated Dimer of T4 Lysozyme R76H/R80H By Synthetic Symmetrization (pdb code 3sb9). 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 Cu-Mediated Dimer of T4 Lysozyme R76H/R80H By Synthetic Symmetrization, PDB code: 3sb9:

Copper binding site 1 out of 1 in the Cu-Mediated Dimer of T4 Lysozyme 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 R76H/R80H By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu163 b:44.0 occ:1.00 NE2 A:HIS80 2.1 43.2 1.0 NE2 B:HIS80 2.1 53.9 1.0 NE2 B:HIS76 2.3 52.3 1.0 O B:HOH181 2.4 37.8 1.0 NE2 A:HIS76 2.4 48.1 1.0 O B:HOH194 2.4 48.3 1.0 CE1 A:HIS80 2.8 47.6 1.0 CE1 B:HIS80 2.8 55.7 1.0 CE1 A:HIS76 2.9 58.9 1.0 CE1 B:HIS76 3.1 60.1 1.0 CD2 A:HIS80 3.3 47.2 1.0 CD2 B:HIS80 3.3 49.0 1.0 CD2 B:HIS76 3.3 46.4 1.0 CD2 A:HIS76 3.5 50.7 1.0 ND1 A:HIS80 4.0 46.2 1.0 ND1 A:HIS76 4.0 54.4 1.0 ND1 B:HIS80 4.0 52.2 1.0 ND1 B:HIS76 4.2 63.8 1.0 CG A:HIS80 4.2 44.8 1.0 CG B:HIS80 4.3 42.9 1.0 CG B:HIS76 4.4 49.0 1.0 CG A:HIS76 4.4 42.3 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