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Atomistry » Chlorine » PDB 3c4x-3ccm » 3c83 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 3c4x-3ccm » 3c83 » |
Chlorine in PDB 3c83: Bacteriophage T4 Lysozyme Mutant D89A in Wildtype Background at Room TemperatureEnzymatic activity of Bacteriophage T4 Lysozyme Mutant D89A in Wildtype Background at Room Temperature
All present enzymatic activity of Bacteriophage T4 Lysozyme Mutant D89A in Wildtype Background at Room Temperature:
3.2.1.17; Protein crystallography data
The structure of Bacteriophage T4 Lysozyme Mutant D89A in Wildtype Background at Room Temperature, PDB code: 3c83
was solved by
B.H.M.Mooers,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Bacteriophage T4 Lysozyme Mutant D89A in Wildtype Background at Room Temperature
(pdb code 3c83). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Bacteriophage T4 Lysozyme Mutant D89A in Wildtype Background at Room Temperature, PDB code: 3c83: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3c83Go back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Bacteriophage T4 Lysozyme Mutant D89A in Wildtype Background at Room Temperature
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 3c83Go back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Bacteriophage T4 Lysozyme Mutant D89A in Wildtype Background at Room Temperature
![]() Mono view ![]() Stereo pair view
Reference:
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.
Page generated: Fri Jul 11 03:41:10 2025
ISSN: ISSN 0961-8368 PubMed: 19384988 DOI: 10.1002/PRO.94 |
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