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Atomistry » Chlorine » PDB 3ccm-3cjx » 3cdq » |
Chlorine in PDB 3cdq: Contributions of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 LysozymeEnzymatic activity of Contributions of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme
All present enzymatic activity of Contributions 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 Contributions of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme, PDB code: 3cdq
was solved by
B.H.M.Mooers,
B.W.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3cdq:
The structure of Contributions 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 Contributions of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme
(pdb code 3cdq). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Contributions of All 20 Amino Acids at Site 96 to the Stability and Structure of T4 Lysozyme, PDB code: 3cdq: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 3cdqGo back to Chlorine Binding Sites List in 3cdq
Chlorine binding site 1 out
of 2 in the Contributions 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 3cdqGo back to Chlorine Binding Sites List in 3cdq
Chlorine binding site 2 out
of 2 in the Contributions 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: Sat Dec 12 09:35:58 2020
ISSN: ISSN 0961-8368 PubMed: 19384988 DOI: 10.1002/PRO.94 |
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