Chlorine in PDB 2b6x: T4 Lysozyme Mutant L99A at 200 Mpa

All present enzymatic activity of T4 Lysozyme Mutant L99A at 200 Mpa:
3.2.1.17;

The structure of T4 Lysozyme Mutant L99A at 200 Mpa, PDB code: 2b6x was solved by M.D.Collins, M.L.Quillin, B.W.Matthews, S.M.Gruner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.49 / 2.11
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.594, 60.594, 95.646, 90.00, 90.00, 120.00
R / Rfree (%)	16.1 / 20.4

The binding sites of Chlorine atom in the T4 Lysozyme Mutant L99A at 200 Mpa (pdb code 2b6x). 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 Mutant L99A at 200 Mpa, PDB code: 2b6x:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant L99A at 200 Mpa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of T4 Lysozyme Mutant L99A at 200 Mpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:36.6 occ:1.00 O A:HOH932 2.7 26.0 1.0 N A:ARG145 3.0 10.1 1.0 N A:ASN144 3.4 11.3 1.0 C A:THR142 3.4 10.8 1.0 CB A:THR142 3.5 11.8 1.0 CB A:ARG145 3.5 10.4 1.0 CA A:THR142 3.5 11.6 1.0 O A:THR142 3.6 11.4 1.0 CB A:ASN144 3.8 13.0 1.0 CA A:ARG145 3.9 10.6 1.0 CA A:ASN144 3.9 12.4 1.0 C A:ASN144 3.9 11.3 1.0 O A:HOH1058 4.0 53.1 1.0 N A:PRO143 4.0 11.4 1.0 C A:PRO143 4.3 11.9 1.0 CG2 A:THR142 4.3 11.2 1.0 O A:HOH952 4.3 29.8 1.0 OG1 A:THR142 4.6 11.6 1.0 CD A:PRO143 4.6 10.0 1.0 CA A:PRO143 4.7 10.9 1.0 O A:HOH959 4.8 33.0 1.0 CG A:ASN144 4.8 18.9 1.0 CG A:ARG145 4.9 13.4 1.0 N A:ALA146 4.9 11.3 1.0 N A:THR142 5.0 11.6 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant L99A at 200 Mpa


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of T4 Lysozyme Mutant L99A at 200 Mpa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:41.1 occ:0.50 O A:HOH938 2.9 16.4 1.0 O A:HOH911 3.0 27.8 1.0 O A:HOH924 3.5 25.2 1.0 CE1 A:HIS31 3.9 11.8 1.0 O A:HOH966 3.9 35.8 1.0 NE2 A:HIS31 4.1 11.4 1.0 CB A:ALA49 4.2 15.7 1.0 NE2 A:GLN69 4.3 12.4 1.0 CA A:ALA49 4.5 15.8 1.0 CD2 A:LEU66 4.6 16.8 1.0 O A:HOH926 4.7 35.7 1.0

M.D.Collins, G.Hummer, M.L.Quillin, B.W.Matthews, S.M.Gruner. Cooperative Water Filling of A Nonpolar Protein Cavity Observed By High-Pressure Crystallography and Simulation Proc.Natl.Acad.Sci.Usa V. 102 16668 2005.
ISSN: ISSN 0027-8424
PubMed: 16269539
DOI: 10.1073/PNAS.0508224102