Chlorine in PDB 1qt7: E11N Mutant of T4 Lysozyme

All present enzymatic activity of E11N Mutant of T4 Lysozyme:
3.2.1.17;

The structure of E11N Mutant of T4 Lysozyme, PDB code: 1qt7 was solved by R.Kuroki, L.H.Weaver, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.078, 61.078, 96.817, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the E11N Mutant of T4 Lysozyme (pdb code 1qt7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the E11N Mutant of T4 Lysozyme, PDB code: 1qt7:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the E11N Mutant of T4 Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of E11N Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:6.7 occ:1.00 O A:HOH209 2.8 44.5 1.0 N A:ARG145 3.3 20.9 1.0 N A:ASN144 3.4 15.1 1.0 C A:THR142 3.4 20.6 1.0 CA A:THR142 3.5 19.9 1.0 CB A:THR142 3.5 23.3 1.0 O A:THR142 3.7 20.3 1.0 CB A:ASN144 3.7 21.9 1.0 CA A:ASN144 3.8 19.9 1.0 N A:PRO143 3.9 22.5 1.0 CB A:ARG145 3.9 21.3 1.0 C A:ASN144 4.1 23.8 1.0 CA A:ARG145 4.2 21.6 1.0 CD A:PRO143 4.2 20.4 1.0 CG2 A:THR142 4.3 23.3 1.0 C A:PRO143 4.3 18.0 1.0 ND2 A:ASN144 4.5 34.5 1.0 CG A:ASN144 4.6 33.5 1.0 O A:HOH230 4.6 48.6 1.0 CA A:PRO143 4.7 19.5 1.0 OG1 A:THR142 4.7 24.4 1.0 O A:HOH245 4.8 53.3 1.0 N A:THR142 4.9 18.2 1.0

Chlorine binding site 2 out of 2 in the E11N Mutant of T4 Lysozyme


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of E11N Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:10.5 occ:0.50 O A:HOH215 2.8 24.5 1.0 O A:HOH182 3.3 27.9 1.0 O A:HOH200 3.4 31.5 1.0 O A:HOH246 3.9 51.2 1.0 CB A:ALA49 4.0 22.4 1.0 CE1 A:HIS31 4.1 23.3 1.0 NE2 A:GLN69 4.1 20.6 1.0 NE2 A:HIS31 4.3 22.3 1.0 CA A:ALA49 4.5 22.5 1.0 CD2 A:LEU66 4.6 29.7 1.0 O A:HOH202 4.6 53.0 1.0 O A:HOH282 4.8 42.6 1.0 O A:ALA49 4.9 22.3 1.0

R.Kuroki, L.H.Weaver, B.W.Matthews. Structural Basis of the Conversion of T4 Lysozyme Into A Transglycosidase By Reengineering the Active Site. Proc.Natl.Acad.Sci.Usa V. 96 8949 1999.
ISSN: ISSN 0027-8424
PubMed: 10430876
DOI: 10.1073/PNAS.96.16.8949