Chlorine in PDB 1cu3: T4 Lysozyme Mutant V87M

All present enzymatic activity of T4 Lysozyme Mutant V87M:
3.2.1.17;

The structure of T4 Lysozyme Mutant V87M, PDB code: 1cu3 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 (°)	60.480, 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 V87M (pdb code 1cu3). 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 V87M, PDB code: 1cu3:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant V87M


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 V87M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:77.8 occ:1.00 N A:ARG145 3.2 6.1 1.0 CB A:THR142 3.5 18.2 1.0 CB A:ARG145 3.6 6.5 1.0 C A:THR142 3.6 14.7 1.0 CA A:THR142 3.6 7.5 1.0 O A:THR142 3.7 9.2 1.0 N A:ASN144 3.8 5.9 1.0 CA A:ARG145 3.9 4.0 1.0 CB A:ASN144 4.0 8.4 1.0 CA A:ASN144 4.2 9.3 1.0 C A:ASN144 4.2 15.2 1.0 N A:PRO143 4.2 11.5 1.0 CG2 A:THR142 4.3 12.2 1.0 O A:HOH324 4.4 30.0 1.0 O A:HOH230 4.4 56.6 1.0 CD A:PRO143 4.5 10.4 1.0 C A:PRO143 4.5 14.4 1.0 OG1 A:THR142 4.6 19.6 1.0 O A:HOH237 4.6 36.7 1.0 CG A:ASN144 4.8 27.2 1.0 ND2 A:ASN144 4.9 47.9 1.0 CA A:PRO143 4.9 13.2 1.0 CG A:ARG145 5.0 22.9 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant V87M


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 V87M within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:49.1 occ:0.50 O A:HOH215 3.0 21.4 1.0 O A:HOH182 3.4 22.0 1.0 O A:HOH200 3.5 30.1 1.0 CE1 A:HIS31 4.1 15.8 1.0 NE2 A:GLN69 4.4 20.3 1.0 NE2 A:HIS31 4.4 19.0 1.0 CB A:ALA49 4.5 16.6 1.0 O A:HOH282 4.7 40.9 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