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Atomistry » Chlorine » PDB 232l-2a65 » 250l » |
Chlorine in PDB 250l: The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic EffectEnzymatic activity of The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect
All present enzymatic activity of The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect:
3.2.1.17; Protein crystallography data
The structure of The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect, PDB code: 250l
was solved by
J.Xu,
W.A.Baase,
E.Baldwin,
B.W.Matthews,
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 The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect
(pdb code 250l). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect, PDB code: 250l: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 250lGo back to Chlorine Binding Sites List in 250l
Chlorine binding site 1 out
of 2 in the The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 250lGo back to Chlorine Binding Sites List in 250l
Chlorine binding site 2 out
of 2 in the The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect
Mono view Stereo pair view
Reference:
J.Xu,
W.A.Baase,
E.Baldwin,
B.W.Matthews.
The Response of T4 Lysozyme to Large-to-Small Substitutions Within the Core and Its Relation to the Hydrophobic Effect. Protein Sci. V. 7 158 1998.
Page generated: Sat Jul 20 05:02:09 2024
ISSN: ISSN 0961-8368 PubMed: 9514271 |
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