Chlorine in PDB 1cv5: T4 Lysozyme Mutant L133M

All present enzymatic activity of T4 Lysozyme Mutant L133M:
3.2.1.17;

The structure of T4 Lysozyme Mutant L133M, PDB code: 1cv5 was solved by N.C.Gassner, W.A.Baase, J.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 / 1.87
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.090, 61.090, 96.990, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the T4 Lysozyme Mutant L133M (pdb code 1cv5). 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 L133M, PDB code: 1cv5:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant L133M


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 L133M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:62.8 occ:1.00 N A:ARG145 3.1 11.1 1.0 CB A:THR142 3.5 17.3 1.0 CB A:ARG145 3.5 10.4 1.0 C A:THR142 3.6 18.5 1.0 N A:ASN144 3.6 8.5 1.0 CA A:THR142 3.6 12.1 1.0 O A:THR142 3.8 14.7 1.0 CA A:ARG145 3.9 12.9 1.0 CB A:ASN144 3.9 9.1 1.0 CA A:ASN144 4.0 9.4 1.0 C A:ASN144 4.0 20.6 1.0 N A:PRO143 4.1 11.8 1.0 CG2 A:THR142 4.3 18.4 1.0 O A:HOH230 4.3 33.5 1.0 C A:PRO143 4.4 15.8 1.0 CD A:PRO143 4.5 14.6 1.0 OG1 A:THR142 4.6 19.3 1.0 O A:HOH237 4.6 40.7 1.0 CA A:PRO143 4.8 13.5 1.0 CG A:ASN144 4.9 27.0 1.0 CG A:ARG145 4.9 19.6 1.0 N A:ALA146 5.0 11.3 1.0 O A:HOH245 5.0 46.5 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant L133M


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 L133M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:41.6 occ:0.50 O A:HOH215 3.0 22.5 1.0 O A:HOH182 3.3 23.0 1.0 O A:HOH200 3.3 37.0 1.0 O A:HOH246 3.6 50.5 1.0 CE1 A:HIS31 4.0 16.8 1.0 CB A:ALA49 4.1 16.0 1.0 NE2 A:HIS31 4.2 15.0 1.0 NE2 A:GLN69 4.3 17.5 1.0 O A:HOH282 4.6 39.3 1.0 CA A:ALA49 4.6 18.3 1.0 O A:HOH202 4.6 56.2 1.0 CD2 A:LEU66 4.7 16.4 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