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Chlorine in PDB 1qt4: T26Q Mutant of T4 Lysozyme

Enzymatic activity of T26Q Mutant of T4 Lysozyme

All present enzymatic activity of T26Q Mutant of T4 Lysozyme:
3.2.1.17;

Protein crystallography data

The structure of T26Q Mutant of T4 Lysozyme, PDB code: 1qt4 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 / 2.10
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.090, 61.090, 96.288, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Chlorine Binding Sites:

The binding sites of Chlorine atom in the T26Q Mutant of T4 Lysozyme (pdb code 1qt4). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the T26Q Mutant of T4 Lysozyme, PDB code: 1qt4:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1qt4

Go back to Chlorine Binding Sites List in 1qt4
Chlorine binding site 1 out of 2 in the T26Q 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 T26Q Mutant of T4 Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl203

b:1.0
occ:1.00
N A:ARG145 3.3 19.7 1.0
N A:ASN144 3.5 12.8 1.0
C A:THR142 3.6 19.1 1.0
CB A:THR142 3.6 22.8 1.0
CA A:THR142 3.6 14.1 1.0
CB A:ASN144 3.7 19.7 1.0
O A:THR142 3.7 18.5 1.0
CB A:ARG145 3.9 16.1 1.0
CA A:ASN144 3.9 14.6 1.0
N A:PRO143 4.1 18.6 1.0
CD A:PRO143 4.1 12.0 1.0
C A:ASN144 4.1 21.8 1.0
CA A:ARG145 4.2 14.8 1.0
CG2 A:THR142 4.3 19.7 1.0
C A:PRO143 4.4 19.3 1.0
ND2 A:ASN144 4.6 28.2 1.0
CG A:ASN144 4.6 29.9 1.0
CA A:PRO143 4.8 18.1 1.0
OG1 A:THR142 4.8 23.4 1.0

Chlorine binding site 2 out of 2 in 1qt4

Go back to Chlorine Binding Sites List in 1qt4
Chlorine binding site 2 out of 2 in the T26Q 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 T26Q Mutant of T4 Lysozyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl207

b:4.0
occ:0.50
O A:HOH261 3.2 60.4 1.0
O A:HOH227 3.4 29.4 1.0
O A:HOH238 3.4 25.1 1.0
O A:HOH211 3.4 24.6 1.0
CE1 A:HIS31 3.9 20.7 1.0
NE2 A:HIS31 4.1 24.1 1.0
CB A:ALA49 4.4 20.1 1.0
O A:HOH282 4.5 55.8 1.0
NE2 A:GLN69 4.5 21.4 1.0
O A:HOH229 4.8 51.5 1.0
CA A:ALA49 4.9 22.8 1.0

Reference:

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
Page generated: Thu Jul 10 19:07:36 2025

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