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Atomistry » Zinc » PDB 3tg0-3ttr » 3tmn » |
Zinc in PDB 3tmn: The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide HydrolysisEnzymatic activity of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
All present enzymatic activity of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis:
3.4.24.27; Protein crystallography data
The structure of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis, PDB code: 3tmn
was solved by
H.M.Holden,
B.W.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3tmn:
The structure of The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
(pdb code 3tmn). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis, PDB code: 3tmn: Zinc binding site 1 out of 1 in 3tmnGo back to Zinc Binding Sites List in 3tmn
Zinc binding site 1 out
of 1 in the The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis
Mono view Stereo pair view
Reference:
H.M.Holden,
B.W.Matthews.
The Binding of L-Valyl-L-Tryptophan to Crystalline Thermolysin Illustrates the Mode of Interaction of A Product of Peptide Hydrolysis. J.Biol.Chem. V. 263 3256 1988.
Page generated: Sat Oct 26 16:38:42 2024
ISSN: ISSN 0021-9258 PubMed: 3343246 |
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