Chlorine in PDB 1cv1: T4 Lysozyme Mutant V111M

All present enzymatic activity of T4 Lysozyme Mutant V111M:
3.2.1.17;

The structure of T4 Lysozyme Mutant V111M, PDB code: 1cv1 was solved by N.C.Gassner, W.A.Baase, J.D.Lindstrom, J.Lu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.10
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.970, 60.970, 97.380, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the T4 Lysozyme Mutant V111M (pdb code 1cv1). 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 V111M, PDB code: 1cv1:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant V111M


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 V111M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:54.8 occ:1.00 O A:HOH209 3.0 41.5 1.0 N A:ARG145 3.0 10.2 1.0 N A:ASN144 3.4 10.3 1.0 CB A:ARG145 3.5 11.9 1.0 CB A:ASN144 3.6 15.4 1.0 C A:THR142 3.6 18.8 1.0 CB A:THR142 3.6 18.3 1.0 O A:THR142 3.7 15.9 1.0 CA A:THR142 3.7 10.1 1.0 CA A:ASN144 3.8 15.9 1.0 CA A:ARG145 3.8 10.0 1.0 C A:ASN144 3.8 19.8 1.0 N A:PRO143 4.1 19.3 1.0 O A:HOH230 4.2 39.5 1.0 C A:PRO143 4.3 19.0 1.0 CG2 A:THR142 4.4 15.9 1.0 CG A:ASN144 4.5 35.9 1.0 CD A:PRO143 4.7 16.4 1.0 OG1 A:THR142 4.8 18.7 1.0 CG A:ARG145 4.8 19.5 1.0 CA A:PRO143 4.8 19.3 1.0 N A:ALA146 4.8 14.3 1.0 ND2 A:ASN144 4.8 52.9 1.0 C A:ARG145 4.9 12.2 1.0 O A:ASN144 5.0 14.0 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant V111M


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 V111M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:45.5 occ:0.50 O A:HOH215 3.0 24.1 1.0 O A:HOH200 3.3 36.5 1.0 O A:HOH182 3.3 23.5 1.0 O A:HOH246 3.9 60.6 1.0 CB A:ALA49 4.0 14.5 1.0 CE1 A:HIS31 4.1 17.7 1.0 NE2 A:HIS31 4.3 16.9 1.0 NE2 A:GLN69 4.3 17.2 1.0 CA A:ALA49 4.4 18.1 1.0 O A:HOH202 4.4 53.2 1.0 CD2 A:LEU66 4.6 28.0 1.0 O A:HOH282 4.6 39.2 1.0 O A:ALA49 5.0 16.6 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