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Zinc in PDB 5h6b: Crystal Structure of A Thermostable Lipase From Marine StreptomycesEnzymatic activity of Crystal Structure of A Thermostable Lipase From Marine Streptomyces
All present enzymatic activity of Crystal Structure of A Thermostable Lipase From Marine Streptomyces:
3.1.1.3; Protein crystallography data
The structure of Crystal Structure of A Thermostable Lipase From Marine Streptomyces, PDB code: 5h6b
was solved by
S.Hou,
Z.Zhao,
J.Liu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of A Thermostable Lipase From Marine Streptomyces
(pdb code 5h6b). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of A Thermostable Lipase From Marine Streptomyces, PDB code: 5h6b: Jump to Zinc binding site number: 1; 2; 3; 4; Zinc binding site 1 out of 4 in 5h6bGo back to![]() ![]()
Zinc binding site 1 out
of 4 in the Crystal Structure of A Thermostable Lipase From Marine Streptomyces
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 4 in 5h6bGo back to![]() ![]()
Zinc binding site 2 out
of 4 in the Crystal Structure of A Thermostable Lipase From Marine Streptomyces
![]() Mono view ![]() Stereo pair view
Zinc binding site 3 out of 4 in 5h6bGo back to![]() ![]()
Zinc binding site 3 out
of 4 in the Crystal Structure of A Thermostable Lipase From Marine Streptomyces
![]() Mono view ![]() Stereo pair view
Zinc binding site 4 out of 4 in 5h6bGo back to![]() ![]()
Zinc binding site 4 out
of 4 in the Crystal Structure of A Thermostable Lipase From Marine Streptomyces
![]() Mono view ![]() Stereo pair view
Reference:
Z.Zhao,
S.Hou,
D.Lan,
X.Wang,
J.Liu,
F.I.Khan,
Y.Wang.
Crystal Structure of A Lipase From Streptomyces Sp. Strain W007 - Implications For Thermostability and Regiospecificity Febs J. V. 284 3506 2017.
Page generated: Sun Oct 27 17:21:42 2024
ISSN: ISSN 1742-4658 PubMed: 28857479 DOI: 10.1111/FEBS.14211 |
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