Chlorine in PDB 1qsq: Cavity Creating Mutation

All present enzymatic activity of Cavity Creating Mutation:
3.2.1.17;

The structure of Cavity Creating Mutation, PDB code: 1qsq was solved by N.C.Gassner, W.A.Baase, J.Lindstrom, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.900, 60.900, 96.500, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Cavity Creating Mutation (pdb code 1qsq). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Cavity Creating Mutation, PDB code: 1qsq:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Cavity Creating Mutation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Cavity Creating Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:37.1 occ:0.50 O A:HOH215 3.0 27.6 1.0 O A:HOH182 3.2 26.4 1.0 O A:HOH200 3.4 31.5 1.0 O A:HOH246 3.5 52.5 1.0 CE1 A:HIS31 4.0 20.9 1.0 CB A:ALA49 4.1 15.8 1.0 NE2 A:HIS31 4.2 17.6 1.0 NE2 A:GLN69 4.3 17.9 1.0 O A:HOH202 4.6 56.1 1.0 CA A:ALA49 4.6 26.3 1.0

Chlorine binding site 2 out of 2 in the Cavity Creating Mutation


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Cavity Creating Mutation within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:37.4 occ:1.00 O A:HOH209 3.1 40.1 1.0 N A:ASN144 3.3 11.1 1.0 N A:ARG145 3.4 15.3 1.0 C A:THR142 3.5 30.3 1.0 CA A:THR142 3.6 13.3 1.0 O A:THR142 3.6 20.6 1.0 CB A:ASN144 3.7 11.9 1.0 CB A:THR142 3.7 20.2 1.0 N A:PRO143 3.9 16.1 1.0 CA A:ASN144 3.9 18.6 1.0 CD A:PRO143 4.0 15.9 1.0 C A:ASN144 4.1 39.3 1.0 CB A:ARG145 4.1 18.8 1.0 C A:PRO143 4.2 17.7 1.0 CA A:ARG145 4.3 22.8 1.0 CG2 A:THR142 4.5 18.9 1.0 CG A:ASN144 4.5 44.0 1.0 CA A:PRO143 4.6 13.1 1.0 ND2 A:ASN144 4.7 22.9 1.0 O A:HOH230 4.9 38.3 1.0 CG A:PRO143 4.9 18.9 1.0 OG1 A:THR142 4.9 25.4 1.0

N.C.Gassner, W.A.Baase, J.D.Lindstrom, J.Lu, F.W.Dahlquist, B.W.Matthews. Methionine and Alanine Substitutions Show That the Formation of Wild-Type-Like Structure in the Carboxy-Terminal Domain of T4 Lysozyme Is A Rate-Limiting Step in Folding. Biochemistry V. 38 14451 1999.
ISSN: ISSN 0006-2960
PubMed: 10545167
DOI: 10.1021/BI9915519