Chlorine in PDB 166l: Control of Enzyme Activity By An Engineered Disulfide Bond

All present enzymatic activity of Control of Enzyme Activity By An Engineered Disulfide Bond:
3.2.1.17;

The structure of Control of Enzyme Activity By An Engineered Disulfide Bond, PDB code: 166l was solved by M.Blaber, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.75
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.840, 60.840, 97.170, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Control of Enzyme Activity By An Engineered Disulfide Bond (pdb code 166l). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Control of Enzyme Activity By An Engineered Disulfide Bond, PDB code: 166l:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Control of Enzyme Activity By An Engineered Disulfide Bond


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Control of Enzyme Activity By An Engineered Disulfide Bond within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:25.5 occ:1.00 O A:HOH209 3.0 25.6 1.0 N A:ASN144 3.3 8.2 1.0 N A:ARG145 3.4 15.1 1.0 C A:THR142 3.5 11.8 1.0 CA A:THR142 3.5 6.4 1.0 CB A:THR142 3.6 15.4 1.0 CB A:ASN144 3.7 7.3 1.0 O A:THR142 3.8 13.2 1.0 CA A:ASN144 3.8 14.8 1.0 N A:PRO143 3.9 14.4 1.0 CB A:ARG145 4.1 17.7 1.0 C A:ASN144 4.1 13.6 1.0 CG2 A:THR142 4.2 10.9 1.0 CD A:PRO143 4.2 15.2 1.0 C A:PRO143 4.3 8.8 1.0 CA A:ARG145 4.4 11.5 1.0 CG A:ASN144 4.6 25.5 1.0 CA A:PRO143 4.7 12.6 1.0 ND2 A:ASN144 4.7 29.7 1.0 O A:HOH230 4.8 23.6 1.0 OG1 A:THR142 4.8 14.2 1.0 N A:THR142 5.0 10.4 1.0

Chlorine binding site 2 out of 2 in the Control of Enzyme Activity By An Engineered Disulfide Bond


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Control of Enzyme Activity By An Engineered Disulfide Bond within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:26.1 occ:0.50 O A:HOH200 3.0 32.3 1.0 O A:HOH215 3.0 24.1 1.0 O A:HOH182 3.5 21.9 1.0 CB A:ALA49 3.8 9.9 1.0 CE1 A:HIS31 4.0 14.1 1.0 O A:HOH282 4.0 29.6 1.0 NE2 A:HIS31 4.2 13.5 1.0 NE2 A:GLN69 4.4 12.2 1.0 CA A:ALA49 4.4 22.4 1.0 CD2 A:LEU66 4.7 19.1 1.0 O A:ALA49 5.0 16.9 1.0

M.Blaber, W.A.Baase, N.Gassner, B.W.Matthews. Alanine Scanning Mutagenesis of the Alpha-Helix 115-123 of Phage T4 Lysozyme: Effects on Structure, Stability and the Binding of Solvent. J.Mol.Biol. V. 246 317 1995.
ISSN: ISSN 0022-2836
PubMed: 7869383
DOI: 10.1006/JMBI.1994.0087