Chlorine in PDB 6pgz: Mtsl Labelled T4 Lysozyme Pseudo-Wild Type V75C Mutant

All present enzymatic activity of Mtsl Labelled T4 Lysozyme Pseudo-Wild Type V75C Mutant:
3.2.1.17;

The structure of Mtsl Labelled T4 Lysozyme Pseudo-Wild Type V75C Mutant, PDB code: 6pgz 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)	14.96 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.941, 53.328, 58.607, 90.00, 102.93, 90.00
R / Rfree (%)	25.3 / 29.1

The binding sites of Chlorine atom in the Mtsl Labelled T4 Lysozyme Pseudo-Wild Type V75C Mutant (pdb code 6pgz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Mtsl Labelled T4 Lysozyme Pseudo-Wild Type V75C Mutant, PDB code: 6pgz:

Chlorine binding site 1 out of 1 in the Mtsl Labelled T4 Lysozyme Pseudo-Wild Type V75C Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mtsl Labelled T4 Lysozyme Pseudo-Wild Type V75C Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:13.9 occ:1.00 O A:HOH311 2.9 24.8 1.0 OH A:TYR88 2.9 11.2 1.0 OH B:TYR88 3.1 15.1 1.0 NH1 A:ARG96 3.3 15.1 1.0 NH1 B:ARG96 3.3 15.9 1.0 CE1 A:TYR88 3.4 11.9 1.0 CE1 B:TYR88 3.5 14.9 1.0 CZ A:TYR88 3.6 14.8 1.0 CZ B:TYR88 3.8 15.4 1.0 C2 A:MTN201 4.0 22.8 1.0 C2 B:MTN300 4.0 15.7 1.0 S1 A:MTN201 4.0 26.9 1.0 CD A:ARG96 4.3 12.2 1.0 CD B:ARG96 4.4 17.2 1.0 S1 B:MTN300 4.4 28.0 1.0 CZ A:ARG96 4.5 13.7 1.0 CZ B:ARG96 4.5 16.0 1.0 CD1 A:TYR88 4.6 10.8 1.0 CD1 B:TYR88 4.8 16.0 1.0 O B:HOH411 4.8 21.0 1.0 C3 A:MTN201 4.8 21.1 1.0 C9 B:MTN300 4.8 16.2 1.0 C1 B:MTN300 4.9 17.6 1.0 NE A:ARG96 4.9 11.7 1.0 C8 A:MTN201 4.9 30.2 1.0 C4 A:MTN201 4.9 20.7 1.0 NE B:ARG96 4.9 13.3 1.0 C3 B:MTN300 4.9 17.9 1.0 C1 A:MTN201 5.0 26.2 1.0 CE2 A:TYR88 5.0 12.7 1.0

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