Copper in PDB 3sb8: Cu-Mediated Dimer of T4 Lysozyme D61H/K65H By Synthetic Symmetrization

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

The structure of Cu-Mediated Dimer of T4 Lysozyme D61H/K65H By Synthetic Symmetrization, PDB code: 3sb8 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)	29.44 / 2.65
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	44.880, 95.180, 117.020, 90.00, 90.00, 90.00
R / Rfree (%)	22.2 / 27.3

The binding sites of Copper atom in the Cu-Mediated Dimer of T4 Lysozyme D61H/K65H By Synthetic Symmetrization (pdb code 3sb8). 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 By Synthetic Symmetrization, PDB code: 3sb8:
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 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 By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu163 b:47.2 occ:1.00 NE2 A:HIS65 2.5 28.9 1.0 NE2 A:GLN69 2.5 33.9 1.0 CA B:GLY-1 2.7 49.1 1.0 CD2 A:HIS65 2.9 21.8 1.0 N B:GLY-1 3.2 32.1 1.0 CD A:GLN69 3.6 31.3 1.0 CE1 A:HIS65 3.7 34.7 1.0 C B:GLY-1 3.7 51.4 1.0 CG A:GLN69 4.2 23.9 1.0 O B:GLY-1 4.2 48.3 1.0 CG A:HIS65 4.2 19.5 1.0 OE1 A:GLN69 4.4 39.8 1.0 ND1 A:HIS65 4.6 23.9 1.0 N B:PRO0 4.6 50.8 1.0 CD B:PRO0 4.8 48.6 1.0

Copper binding site 2 out of 2 in the Cu-Mediated Dimer of T4 Lysozyme D61H/K65H 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 By Synthetic Symmetrization within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu163 b:46.1 occ:1.00 NE2 B:HIS65 2.4 34.9 1.0 N A:GLY-1 2.5 52.8 1.0 CD2 B:HIS65 2.8 27.6 1.0 CA A:GLY-1 2.9 41.5 1.0 NE2 B:GLN69 2.9 38.8 1.0 C A:GLY-2 3.2 58.4 1.0 OE1 B:GLN69 3.5 34.1 1.0 CD B:GLN69 3.5 32.5 1.0 CE1 B:HIS65 3.6 38.0 1.0 CA A:GLY-2 3.7 52.4 1.0 N A:GLY-2 3.7 47.7 1.0 C A:GLY-1 3.8 50.0 1.0 O A:GLY-2 4.0 60.2 1.0 O A:GLY-1 4.1 47.2 1.0 CG B:HIS65 4.2 27.4 1.0 ND1 B:HIS65 4.5 34.3 1.0 CG B:GLN69 4.8 35.0 1.0 N A:PRO0 4.8 46.4 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