Chlorine in PDB 1qt3: T26D Mutant of T4 Lysozyme

All present enzymatic activity of T26D Mutant of T4 Lysozyme:
3.2.1.17;

The structure of T26D Mutant of T4 Lysozyme, PDB code: 1qt3 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 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	60.900, 60.900, 96.900, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Chlorine atom in the T26D Mutant of T4 Lysozyme (pdb code 1qt3). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the T26D Mutant of T4 Lysozyme, PDB code: 1qt3:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the T26D 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 T26D Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:1.0 occ:1.00 O A:HOH237 2.8 22.8 1.0 N A:ARG145 3.3 12.6 1.0 N A:ASN144 3.4 7.0 1.0 CA A:THR142 3.5 9.6 1.0 C A:THR142 3.5 13.4 1.0 CB A:THR142 3.7 13.2 1.0 CB A:ASN144 3.7 15.2 1.0 O A:THR142 3.9 14.2 1.0 CA A:ASN144 3.9 12.8 1.0 N A:PRO143 3.9 15.1 1.0 CB A:ARG145 4.0 11.3 1.0 C A:ASN144 4.1 15.1 1.0 CD A:PRO143 4.1 12.6 1.0 CA A:ARG145 4.2 12.6 1.0 CG2 A:THR142 4.3 12.7 1.0 C A:PRO143 4.4 13.0 1.0 O A:HOH256 4.5 34.0 1.0 ND2 A:ASN144 4.5 29.0 1.0 CG A:ASN144 4.6 27.7 1.0 CA A:PRO143 4.7 13.8 1.0 OG1 A:THR142 4.9 14.6 1.0 N A:THR142 4.9 14.7 1.0

Chlorine binding site 2 out of 2 in the T26D 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 T26D Mutant of T4 Lysozyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl208 b:2.5 occ:0.50 O A:HOH242 2.9 17.6 1.0 O A:HOH229 3.3 26.3 1.0 O A:HOH212 3.3 22.8 1.0 CB A:ALA49 4.0 13.2 1.0 O A:HOH270 4.1 49.1 1.0 CE1 A:HIS31 4.2 13.1 1.0 NE2 A:HIS31 4.3 13.5 1.0 O A:HOH301 4.4 49.1 1.0 NE2 A:GLN69 4.4 15.5 1.0 CA A:ALA49 4.5 18.7 1.0 O A:HOH231 4.7 55.7 1.0 CD2 A:LEU66 4.7 14.8 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