Chlorine in PDB 1cx6: T4 Lysozyme Substituted with Selenomethionine

All present enzymatic activity of T4 Lysozyme Substituted with Selenomethionine:
3.2.1.17;

The structure of T4 Lysozyme Substituted with Selenomethionine, PDB code: 1cx6 was solved by N.C.Gassner, W.A.Baase, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.01
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.400, 61.400, 96.700, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the T4 Lysozyme Substituted with Selenomethionine (pdb code 1cx6). 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 Substituted with Selenomethionine, PDB code: 1cx6:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Substituted with Selenomethionine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of T4 Lysozyme Substituted with Selenomethionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:9.0 occ:1.00 O A:HOH331 2.7 24.6 1.0 O A:HOH201 2.8 54.2 1.0 N A:ARG145 3.0 11.0 1.0 N A:ASN144 3.5 9.2 1.0 CB A:ARG145 3.6 13.6 1.0 C A:THR142 3.7 14.2 1.0 CB A:ASN144 3.7 11.1 1.0 CA A:ASN144 3.8 8.3 1.0 C A:ASN144 3.8 21.7 1.0 CB A:THR142 3.8 13.8 1.0 CA A:ARG145 3.9 7.3 1.0 O A:THR142 3.9 18.0 1.0 CA A:THR142 3.9 7.6 1.0 O A:HOH214 3.9 50.6 1.0 N A:PRO143 4.1 11.9 1.0 O A:HOH328 4.3 38.6 1.0 C A:PRO143 4.4 13.6 1.0 CD A:PRO143 4.6 9.6 1.0 CG A:ASN144 4.7 24.8 1.0 OG1 A:THR142 4.8 13.9 1.0 CA A:PRO143 4.8 7.4 1.0 CG2 A:THR142 4.8 13.9 1.0 ND2 A:ASN144 4.9 31.4 1.0 O A:ASN144 5.0 12.6 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Substituted with Selenomethionine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of T4 Lysozyme Substituted with Selenomethionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl177 b:1.6 occ:0.50 O A:HOH205 2.9 19.9 1.0 O A:HOH195 3.2 40.5 1.0 O A:HOH181 3.2 25.4 1.0 O A:HOH226 3.6 51.6 1.0 CB A:ALA49 3.8 14.8 1.0 CE1 A:HIS31 3.9 15.0 1.0 NE2 A:HIS31 3.9 14.7 1.0 NE2 A:GLN69 4.3 14.7 1.0 CA A:ALA49 4.5 14.8 1.0 CD2 A:LEU66 4.5 19.1 1.0 O A:HOH241 4.5 35.5 1.0

N.C.Gassner, W.A.Baase, A.C.Hausrath, B.W.Matthews. Substitution with Selenomethionine Can Enhance the Stability of Methionine-Rich Proteins. J.Mol.Biol. V. 294 17 1999.
ISSN: ISSN 0022-2836
PubMed: 10556025
DOI: 10.1006/JMBI.1999.3220