Chlorine in PDB 1cu0: T4 Lysozyme Mutant I78M

All present enzymatic activity of T4 Lysozyme Mutant I78M:
3.2.1.17;

The structure of T4 Lysozyme Mutant I78M, PDB code: 1cu0 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 / 2.20
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.480, 60.480, 97.700, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the T4 Lysozyme Mutant I78M (pdb code 1cu0). 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 I78M, PDB code: 1cu0:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant I78M


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 I78M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:44.4 occ:1.00 O A:HOH209 3.0 71.0 1.0 N A:ASN144 3.4 17.5 1.0 N A:ARG145 3.4 21.6 1.0 C A:THR142 3.4 30.6 1.0 CA A:THR142 3.5 25.2 1.0 CB A:THR142 3.6 41.0 1.0 CB A:ASN144 3.6 24.6 1.0 O A:THR142 3.7 24.6 1.0 N A:PRO143 3.8 33.3 1.0 CA A:ASN144 3.8 27.3 1.0 CD A:PRO143 3.9 17.4 1.0 CB A:ARG145 4.0 26.2 1.0 C A:ASN144 4.1 22.3 1.0 CG2 A:THR142 4.2 22.3 1.0 CA A:ARG145 4.3 27.2 1.0 C A:PRO143 4.3 27.3 1.0 CG A:ASN144 4.5 51.5 1.0 ND2 A:ASN144 4.5 34.5 1.0 CA A:PRO143 4.6 34.5 1.0 OG1 A:THR142 4.8 28.5 1.0 CG A:PRO143 4.8 28.0 1.0 N A:THR142 4.9 21.6 1.0 O A:HOH330 4.9 49.2 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant I78M


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 I78M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:47.6 occ:0.50 O A:HOH215 3.1 35.3 1.0 O A:HOH182 3.3 35.5 1.0 O A:HOH200 3.9 58.9 1.0 CB A:ALA49 4.0 24.4 1.0 CE1 A:HIS31 4.2 21.9 1.0 O A:HOH282 4.4 49.2 1.0 NE2 A:GLN69 4.4 33.1 1.0 NE2 A:HIS31 4.4 34.8 1.0 CA A:ALA49 4.5 29.9 1.0 CD2 A:LEU66 4.6 32.4 1.0 O A:HOH202 4.9 62.8 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