Chlorine in PDB 1qt6: E11H Mutant of T4 Lysozyme

All present enzymatic activity of E11H Mutant of T4 Lysozyme:
3.2.1.17;

The structure of E11H Mutant of T4 Lysozyme, PDB code: 1qt6 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 / 1.90
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.080, 61.080, 96.760, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the E11H Mutant of T4 Lysozyme (pdb code 1qt6). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the E11H Mutant of T4 Lysozyme, PDB code: 1qt6:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the E11H 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 E11H Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl173 b:5.9 occ:1.00 N A:ARG145 3.3 23.7 1.0 N A:ASN144 3.3 20.5 1.0 C A:THR142 3.5 25.3 1.0 CB A:THR142 3.5 23.8 1.0 CA A:THR142 3.5 21.1 1.0 CB A:ASN144 3.6 27.9 1.0 O A:THR142 3.8 24.4 1.0 CA A:ASN144 3.8 23.4 1.0 N A:PRO143 3.9 25.7 1.0 CB A:ARG145 3.9 26.4 1.0 C A:ASN144 4.0 25.4 1.0 CD A:PRO143 4.1 23.1 1.0 CG2 A:THR142 4.1 23.1 1.0 CA A:ARG145 4.2 21.3 1.0 C A:PRO143 4.3 22.5 1.0 CG A:ASN144 4.5 36.8 1.0 CA A:PRO143 4.6 21.3 1.0 ND2 A:ASN144 4.6 37.8 1.0 OG1 A:THR142 4.7 26.6 1.0 O A:HOH304 4.9 0.0 1.0 N A:THR142 4.9 20.4 1.0

Chlorine binding site 2 out of 2 in the E11H 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 E11H Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl178 b:6.3 occ:0.50 O A:HOH215 2.9 22.8 1.0 O A:HOH182 3.3 28.2 1.0 O A:HOH200 3.5 36.6 1.0 CB A:ALA49 3.9 22.9 1.0 CE1 A:HIS31 4.0 24.0 1.0 O A:HOH246 4.2 71.8 1.0 NE2 A:HIS31 4.2 26.3 1.0 NE2 A:GLN69 4.3 23.0 1.0 CA A:ALA49 4.5 24.3 1.0 O A:HOH282 4.6 45.0 1.0 CD2 A:LEU66 4.6 26.3 1.0 O A:HOH202 4.7 71.5 1.0 O A:ALA49 4.9 25.5 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