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Atomistry » Calcium » PDB 8hcj-8ic1 » 8ibm » |
Calcium in PDB 8ibm: Sulfate Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability-Improving Mutations of S226P/R228S/Q138A/D250C- E296C/Q123H/N202H and S176A InactivationEnzymatic activity of Sulfate Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability-Improving Mutations of S226P/R228S/Q138A/D250C- E296C/Q123H/N202H and S176A Inactivation
All present enzymatic activity of Sulfate Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability-Improving Mutations of S226P/R228S/Q138A/D250C- E296C/Q123H/N202H and S176A Inactivation:
3.1.1.74; Protein crystallography data
The structure of Sulfate Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability-Improving Mutations of S226P/R228S/Q138A/D250C- E296C/Q123H/N202H and S176A Inactivation, PDB code: 8ibm
was solved by
M.Emori,
N.Numoto,
N.Kamiya,
M.Oda,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Sulfate Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability-Improving Mutations of S226P/R228S/Q138A/D250C- E296C/Q123H/N202H and S176A Inactivation
(pdb code 8ibm). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Sulfate Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability-Improving Mutations of S226P/R228S/Q138A/D250C- E296C/Q123H/N202H and S176A Inactivation, PDB code: 8ibm: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 8ibmGo back to![]() ![]()
Calcium binding site 1 out
of 2 in the Sulfate Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability-Improving Mutations of S226P/R228S/Q138A/D250C- E296C/Q123H/N202H and S176A Inactivation
![]() Mono view ![]() Stereo pair view
Calcium binding site 2 out of 2 in 8ibmGo back to![]() ![]()
Calcium binding site 2 out
of 2 in the Sulfate Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability-Improving Mutations of S226P/R228S/Q138A/D250C- E296C/Q123H/N202H and S176A Inactivation
![]() Mono view ![]() Stereo pair view
Reference:
N.Numoto,
N.Kamiya,
M.Oda.
Improvement of Thermostability and Activity of Pet-Degrading Enzyme CUT190 Towards A Detailed Understanding and Application of the Enzymatic Reaction Mechanism. Biorxiv 2023.
Page generated: Thu Jul 10 05:12:34 2025
ISSN: ISSN 2692-8205 DOI: 10.1101/2023.02.26.529345 |
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