Chlorine in PDB 1cv0: T4 Lysozyme Mutant F104M

All present enzymatic activity of T4 Lysozyme Mutant F104M:
3.2.1.17;

The structure of T4 Lysozyme Mutant F104M, PDB code: 1cv0 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 / 2.12
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.860, 60.860, 97.200, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the T4 Lysozyme Mutant F104M (pdb code 1cv0). 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 F104M, PDB code: 1cv0:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant F104M


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 F104M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:27.5 occ:1.00 O A:HOH209 3.0 26.7 1.0 N A:ASN144 3.3 1.0 1.0 N A:ARG145 3.3 19.6 1.0 C A:THR142 3.4 18.0 1.0 CA A:THR142 3.5 9.1 1.0 CB A:THR142 3.5 19.8 1.0 CB A:ASN144 3.7 8.9 1.0 N A:PRO143 3.7 16.8 1.0 O A:THR142 3.8 11.5 1.0 CA A:ASN144 3.9 12.2 1.0 CB A:ARG145 3.9 8.9 1.0 CD A:PRO143 4.1 14.6 1.0 C A:ASN144 4.1 15.6 1.0 C A:PRO143 4.1 9.0 1.0 CA A:ARG145 4.2 14.4 1.0 CG2 A:THR142 4.2 12.6 1.0 ND2 A:ASN144 4.3 41.5 1.0 CG A:ASN144 4.5 40.0 1.0 CA A:PRO143 4.5 11.5 1.0 OG1 A:THR142 4.7 17.2 1.0 N A:THR142 4.9 5.3 1.0 CG A:PRO143 4.9 9.7 1.0 O A:HOH230 5.0 25.7 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant F104M


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 F104M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:37.8 occ:0.50 O A:HOH215 3.2 20.7 1.0 O A:HOH182 3.4 23.6 1.0 O A:HOH200 3.9 44.6 1.0 CE1 A:HIS31 4.2 9.8 1.0 O A:HOH202 4.3 43.6 1.0 NE2 A:HIS31 4.3 11.6 1.0 NE2 A:GLN69 4.5 13.1 1.0 O A:HOH282 4.5 54.6 1.0 CB A:ALA49 4.5 13.4 1.0 CA A:ALA49 4.8 16.6 1.0 O A:HOH246 4.8 65.0 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