Chlorine in PDB 8ibl: Mes Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation

Enzymatic activity of Mes 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 Mes 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 Mes Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation, PDB code: 8ibl 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:

Resolution Low / High (Å) 32.36 / 2.60
Space group P 3
Cell size a, b, c (Å), α, β, γ (°) 83.869, 83.869, 64.723, 90, 90, 120
R / Rfree (%) 21.1 / 26.3

Other elements in 8ibl:

The structure of Mes Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Mes Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation (pdb code 8ibl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Mes Bound Form of Pet-Degrading Cutinase CUT190 with Thermostability- Improving Mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A Inactivation, PDB code: 8ibl:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 8ibl

Go back to Chlorine Binding Sites List in 8ibl
Chlorine binding site 1 out of 2 in the Mes 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

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Mes Bound 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:Cl403

b:44.4
occ:1.00
 OG A:SER76 3.8 37.1 1.0
N A:SER76 3.8 35.0 1.0
NE A:ARG73 4.1 49.7 1.0
CA A:SER75 4.1 37.9 1.0
CB A:SER76 4.4 32.0 1.0
CB A:SER75 4.4 36.3 1.0
C A:SER75 4.5 39.2 1.0
OG A:SER75 4.5 31.7 1.0
CD A:ARG73 4.7 47.5 1.0
NH2 A:ARG73 4.7 58.9 1.0
CA A:SER76 4.7 38.8 1.0
CZ A:ARG73 4.8 51.1 1.0
O A:HOH501 4.9 24.0 1.0

Chlorine binding site 2 out of 2 in 8ibl

Go back to Chlorine Binding Sites List in 8ibl
Chlorine binding site 2 out of 2 in the Mes 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

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Mes Bound 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
B:Cl403

b:43.7
occ:1.00
 OG B:SER76 3.6 35.1 1.0
N B:SER76 3.9 28.6 1.0
NE B:ARG73 4.3 50.6 1.0
CB B:SER76 4.3 30.4 1.0
CA B:SER75 4.4 35.7 1.0
C B:SER75 4.7 34.9 1.0
O B:HOH503 4.7 20.7 1.0
CA B:SER76 4.7 32.7 1.0
OG B:SER75 4.8 36.6 1.0
CB B:SER75 4.8 33.3 1.0
O B:HOH521 4.9 32.8 1.0
NH2 B:ARG73 4.9 52.8 1.0
CD B:ARG73 4.9 50.9 1.0

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.
ISSN: ISSN 2692-8205
DOI: 10.1101/2023.02.26.529345
Page generated: Tue Apr 4 22:58:36 2023

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