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Zinc in PDB 8tln: Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During CatalysisEnzymatic activity of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis
All present enzymatic activity of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis:
3.4.24.27; Protein crystallography data
The structure of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis, PDB code: 8tln
was solved by
D.Tronrud,
B.W.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 8tln:
The structure of Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis
(pdb code 8tln). 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 Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis, PDB code: 8tln: Zinc binding site 1 out of 1 in 8tlnGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis
![]() Mono view ![]() Stereo pair view
Reference:
D.R.Holland,
D.E.Tronrud,
H.W.Pley,
K.M.Flaherty,
W.Stark,
J.N.Jansonius,
D.B.Mckay,
B.W.Matthews.
Structural Comparison Suggests That Thermolysin and Related Neutral Proteases Undergo Hinge-Bending Motion During Catalysis. Biochemistry V. 31 11310 1992.
Page generated: Wed Dec 16 14:05:16 2020
ISSN: ISSN 0006-2960 PubMed: 1445869 DOI: 10.1021/BI00161A008 |
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