Chlorine in PDB 3c7z: T4 Lysozyme Mutant D89A/R96H at Room Temperature

All present enzymatic activity of T4 Lysozyme Mutant D89A/R96H at Room Temperature:
3.2.1.17;

The structure of T4 Lysozyme Mutant D89A/R96H at Room Temperature, PDB code: 3c7z was solved by B.H.M.Mooers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	11.44 / 1.67
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.942, 60.942, 96.813, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the T4 Lysozyme Mutant D89A/R96H at Room Temperature (pdb code 3c7z). 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 D89A/R96H at Room Temperature, PDB code: 3c7z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T4 Lysozyme Mutant D89A/R96H at Room Temperature


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 D89A/R96H at Room Temperature within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl168 b:41.9 occ:1.00 O A:HOH209 3.1 34.8 1.0 N A:ARG145 3.1 10.1 1.0 N A:ASN144 3.3 8.9 1.0 C A:THR142 3.5 13.9 1.0 CA A:THR142 3.6 10.1 1.0 CB A:THR142 3.6 11.8 1.0 O A:THR142 3.7 13.5 1.0 CB A:ASN144 3.7 15.1 1.0 CA A:ASN144 3.7 12.4 1.0 N A:PRO143 3.9 13.5 1.0 CB A:ARG145 3.9 18.8 1.0 C A:ASN144 3.9 19.4 1.0 CA A:ARG145 4.1 11.3 1.0 C A:PRO143 4.2 12.3 1.0 CD A:PRO143 4.3 18.0 1.0 CG2 A:THR142 4.4 13.6 1.0 O A:HOH230 4.6 36.3 1.0 CA A:PRO143 4.6 13.0 1.0 CG A:ASN144 4.7 32.2 1.0 OG1 A:THR142 4.8 18.6 1.0 OD1 A:ASN144 4.9 34.2 1.0 CG A:PRO143 5.0 15.2 1.0

Chlorine binding site 2 out of 2 in the T4 Lysozyme Mutant D89A/R96H at Room Temperature


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 D89A/R96H at Room Temperature within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:36.9 occ:0.50 O A:HOH215 3.0 18.2 1.0 C A:LYS135 3.7 14.2 1.0 N A:SER136 3.8 11.1 1.0 CA A:LYS135 3.9 13.5 1.0 OD1 A:ASN140 4.0 27.8 1.0 O A:LYS135 4.2 17.4 1.0 CB A:LYS135 4.3 16.6 1.0 CA A:SER136 4.5 15.5 1.0 O A:HOH282 4.6 35.4 1.0 C A:SER136 4.7 10.0 1.0 O A:SER136 4.8 14.0 1.0 O A:ALA134 5.0 15.1 1.0

B.H.Mooers, W.A.Baase, J.W.Wray, B.W.Matthews. Contributions of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme. Protein Sci. V. 18 871 2009.
ISSN: ISSN 0961-8368
PubMed: 19384988
DOI: 10.1002/PRO.94