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Atomistry » Chlorine » PDB 3c4x-3ccm » 3c8q » |
Chlorine in PDB 3c8q: Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 LysozymeEnzymatic activity of Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme
All present enzymatic activity of Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme:
3.2.1.17; Protein crystallography data
The structure of Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme, PDB code: 3c8q
was solved by
B.H.M.Mooers,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3c8q:
The structure of Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme
(pdb code 3c8q). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme, PDB code: 3c8q: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3c8qGo back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 3c8qGo back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Contribution of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme
![]() 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 03:41:30 2025
ISSN: ISSN 0961-8368 PubMed: 19384988 DOI: 10.1002/PRO.94 |
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