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Atomistry » Potassium » PDB 1k4d-1m40 » 1lwg » |
Potassium in PDB 1lwg: Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and StabilityEnzymatic activity of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability
All present enzymatic activity of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability:
3.2.1.17; Protein crystallography data
The structure of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability, PDB code: 1lwg
was solved by
N.C.Gassner,
W.A.Baase,
B.H.M.Mooers,
R.D.Busam,
L.H.Weaver,
J.D.Lindstrom,
M.L.Quillin,
B.M.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1lwg:
The structure of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability
(pdb code 1lwg). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability, PDB code: 1lwg: Potassium binding site 1 out of 1 in 1lwgGo back to Potassium Binding Sites List in 1lwg
Potassium binding site 1 out
of 1 in the Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability
Mono view Stereo pair view
Reference:
N.C.Gassner,
W.A.Baase,
B.H.Mooers,
R.D.Busam,
L.H.Weaver,
J.D.Lindstrom,
M.L.Quillin,
B.W.Matthews.
Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability. Biophys.Chem. V. 100 325 2003.
Page generated: Mon Aug 12 04:52:58 2024
ISSN: ISSN 0301-4622 PubMed: 12646375 DOI: 10.1016/S0301-4622(02)00290-9 |
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