Chlorine in PDB 6ph1: T4 Lysozyme Pseudo-Wild Type Soaked in Tempol

All present enzymatic activity of T4 Lysozyme Pseudo-Wild Type Soaked in Tempol:
3.2.1.17;

The structure of T4 Lysozyme Pseudo-Wild Type Soaked in Tempol, PDB code: 6ph1 was solved by M.J.Cuneo, D.A.Myles, L.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.88 / 1.63
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.165, 60.165, 95.720, 90.00, 90.00, 120.00
R / Rfree (%)	16.7 / 19.6

The binding sites of Chlorine atom in the T4 Lysozyme Pseudo-Wild Type Soaked in Tempol (pdb code 6ph1). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the T4 Lysozyme Pseudo-Wild Type Soaked in Tempol, PDB code: 6ph1:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Pseudo-Wild Type Soaked in Tempol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of T4 Lysozyme Pseudo-Wild Type Soaked in Tempol within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:25.0 occ:1.00 O A:HOH551 3.0 18.6 1.0 N A:ARG145 3.1 13.8 1.0 N A:ASN144 3.3 14.5 1.0 C A:THR142 3.4 14.2 1.0 CA A:THR142 3.4 13.7 1.0 CB A:THR142 3.6 15.4 1.0 N A:PRO143 3.7 11.9 1.0 O A:THR142 3.7 14.0 1.0 CB A:ARG145 3.7 16.2 1.0 CB A:ASN144 3.8 13.2 1.0 CA A:ASN144 3.9 13.5 1.0 C A:ASN144 4.0 14.9 1.0 CA A:ARG145 4.1 12.0 1.0 CD A:PRO143 4.2 15.4 1.0 C A:PRO143 4.2 14.5 1.0 CG2 A:THR142 4.3 15.3 1.0 CA A:PRO143 4.5 11.7 1.0 O A:HOH378 4.7 22.3 1.0 OG1 A:THR142 4.7 15.7 1.0 CG A:ASN144 4.8 18.2 1.0 N A:THR142 4.8 13.5 1.0 CG A:PRO143 5.0 13.6 1.0 O A:HOH391 5.0 24.7 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Pseudo-Wild Type Soaked in Tempol


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of T4 Lysozyme Pseudo-Wild Type Soaked in Tempol within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:0.2 occ:1.00 O A:HOH529 2.1 36.2 1.0 O A:HOH334 3.4 24.2 1.0 CE1 A:HIS31 3.6 14.3 1.0 NE2 A:HIS31 4.0 13.8 1.0 O A:HOH430 4.2 19.0 1.0 O A:HOH419 4.4 28.7 1.0 O A:HOH335 4.5 25.5 1.0 ND1 A:HIS31 4.8 15.8 1.0 OD1 A:ASP70 4.9 16.3 1.0

J.Pierce, D.A.Myles. Making Hydrogens Stand Out: Enhanced Neutron Diffraction From Biological Crystals Using Dynamic Nuclear Polarization To Be Published.