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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 Inactivation

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

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:

Resolution Low / High (Å) 30.02 / 1.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 62.623, 64.984, 78.453, 90, 90, 90
R / Rfree (%) 14.2 / 16.2

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 7cts

Go back to Calcium Binding Sites List in 7cts
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

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Open Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca503

b:19.0
occ:1.00
 O A:SER76 2.3 16.3 1.0
O A:ALA78 2.3 15.3 1.0
O A:PHE81 2.3 12.4 1.0
O A:HOH892 2.3 20.5 1.0
O A:HOH656 2.4 24.1 1.0
O A:HOH894 2.6 20.0 1.0
C A:SER76 3.4 15.4 1.0
C A:ALA78 3.5 15.2 1.0
C A:PHE81 3.5 11.3 1.0
C A:PHE77 3.8 17.0 1.0
N A:ALA78 3.8 15.7 1.0
CA A:PHE77 4.0 17.7 1.0
N A:PHE81 4.0 11.9 1.0
N A:PHE77 4.2 15.6 1.0
O A:PHE77 4.2 17.9 1.0
CA A:ALA78 4.2 15.2 1.0
OD1 A:ASN133 4.3 16.4 1.0
CA A:GLY82 4.3 12.6 1.0
N A:GLY82 4.3 11.7 1.0
CA A:SER76 4.4 15.8 1.0
N A:GLY80 4.4 13.5 1.0
CA A:PHE81 4.4 12.0 1.0
N A:SER79 4.5 16.8 1.0
O A:HOH960 4.6 29.7 1.0
O A:HOH1030 4.6 30.8 1.0
O A:HOH834 4.6 30.1 1.0
C A:SER79 4.7 14.5 1.0
CA A:SER79 4.7 17.5 1.0
C A:GLY82 4.8 12.8 1.0
N A:GLY83 4.8 12.6 1.0
CB A:ALA78 4.9 15.5 1.0

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.
ISSN: ESSN 1097-0134
PubMed: 33340163
DOI: 10.1002/PROT.26034
Page generated: Wed Jul 9 21:25:29 2025

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