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Atomistry » Calcium » PDB 7cji-7d4p » 7cts » |
Calcium in PDB 7cts: Open Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A InactivationEnzymatic activity of Open 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 Open 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 Open Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation, PDB code: 7cts
was solved by
M.Emori,
N.Numoto,
A.Senga,
G.J.Bekker,
N.Kamiya,
N.Ito,
F.Kawai,
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 Open Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation
(pdb code 7cts). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Open Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation, PDB code: 7cts: Calcium binding site 1 out of 1 in 7ctsGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Open 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:
M.Emori,
N.Numoto,
A.Senga,
G.J.Bekker,
N.Kamiya,
Y.Kobayashi,
N.Ito,
F.Kawai,
M.Oda.
Structural Basis of Mutants of Pet-Degrading Enzyme From Saccharomonospora Viridis AHK190 with High Activity and Thermal Stability. Proteins 2020.
Page generated: Thu Jul 18 23:51:08 2024
ISSN: ESSN 1097-0134 PubMed: 33340163 DOI: 10.1002/PROT.26034 |
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