Chlorine in PDB 3c7y: Mutant R96A of T4 Lysozyme in Wildtype Background at 298K

All present enzymatic activity of Mutant R96A of T4 Lysozyme in Wildtype Background at 298K:
3.2.1.17;

The structure of Mutant R96A of T4 Lysozyme in Wildtype Background at 298K, PDB code: 3c7y 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)	24.00 / 1.95
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.039, 61.039, 97.092, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the Mutant R96A of T4 Lysozyme in Wildtype Background at 298K (pdb code 3c7y). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Mutant R96A of T4 Lysozyme in Wildtype Background at 298K, PDB code: 3c7y:

Chlorine binding site 1 out of 1 in the Mutant R96A of T4 Lysozyme in Wildtype Background at 298K


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mutant R96A of T4 Lysozyme in Wildtype Background at 298K within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl168 b:35.0 occ:1.00 O A:HOH624 3.0 30.6 1.0 N A:ARG145 3.2 14.1 1.0 N A:ASN144 3.4 7.1 1.0 C A:THR142 3.4 15.2 1.0 CA A:THR142 3.5 6.6 1.0 CB A:THR142 3.5 11.7 1.0 N A:PRO143 3.7 13.2 1.0 CB A:ARG145 3.8 11.2 1.0 O A:THR142 3.8 13.9 1.0 CB A:ASN144 3.9 5.1 1.0 O A:HOH653 3.9 34.0 1.0 CA A:ASN144 3.9 9.5 1.0 C A:ASN144 4.0 19.1 1.0 CA A:ARG145 4.0 14.1 1.0 C A:PRO143 4.2 16.5 1.0 CD A:PRO143 4.3 13.1 1.0 CG2 A:THR142 4.3 12.9 1.0 CA A:PRO143 4.5 17.6 1.0 O A:HOH634 4.6 34.7 1.0 OG1 A:THR142 4.6 13.5 1.0 O A:HOH636 4.8 29.4 1.0 CG A:PRO143 4.9 16.5 1.0 OD1 A:ASN144 4.9 33.2 1.0 N A:THR142 4.9 11.8 1.0 CG A:ASN144 4.9 32.4 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