Chlorine in PDB 1cu2: T4 Lysozyme Mutant L84M

All present enzymatic activity of T4 Lysozyme Mutant L84M:
3.2.1.17;

The structure of T4 Lysozyme Mutant L84M, PDB code: 1cu2 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 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.070, 61.070, 96.850, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the T4 Lysozyme Mutant L84M (pdb code 1cu2). 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 L84M, PDB code: 1cu2:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant L84M


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 L84M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:52.0 occ:1.00 O A:HOH209 2.9 43.5 1.0 N A:ARG145 3.0 13.2 1.0 N A:ASN144 3.3 7.9 1.0 C A:THR142 3.4 19.6 1.0 CB A:THR142 3.5 19.8 1.0 CB A:ARG145 3.5 14.8 1.0 CA A:THR142 3.5 11.9 1.0 O A:THR142 3.5 14.7 1.0 CB A:ASN144 3.6 14.9 1.0 CA A:ASN144 3.7 14.3 1.0 C A:ASN144 3.8 23.4 1.0 CA A:ARG145 3.8 12.0 1.0 N A:PRO143 3.9 15.9 1.0 C A:PRO143 4.1 16.2 1.0 CG2 A:THR142 4.3 17.6 1.0 O A:HOH245 4.3 39.8 1.0 O A:HOH230 4.4 36.0 1.0 CD A:PRO143 4.5 17.2 1.0 CG A:ASN144 4.6 35.2 1.0 OG1 A:THR142 4.6 17.9 1.0 CA A:PRO143 4.7 12.0 1.0 N A:ALA146 4.8 14.4 1.0 ND2 A:ASN144 4.9 34.3 1.0 C A:ARG145 4.9 13.3 1.0 CG A:ARG145 4.9 18.6 1.0 O A:ASN144 4.9 14.4 1.0 N A:THR142 5.0 13.4 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant L84M


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 L84M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:46.9 occ:0.50 O A:HOH215 2.9 23.1 1.0 O A:HOH200 3.3 34.9 1.0 O A:HOH182 3.3 25.0 1.0 CB A:ALA49 3.7 17.8 1.0 O A:HOH246 4.0 51.6 1.0 CE1 A:HIS31 4.1 17.6 1.0 CA A:ALA49 4.2 20.8 1.0 NE2 A:HIS31 4.3 15.6 1.0 NE2 A:GLN69 4.3 16.7 1.0 O A:HOH282 4.4 34.2 1.0 CD2 A:LEU66 4.5 20.7 1.0 O A:HOH202 4.6 68.1 1.0 O A:ALA49 4.7 18.2 1.0 C A:ALA49 5.0 19.2 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