Download MendeleyImprovement of thermostability and activity of PET-degrading enzyme Cut190 towards a detailed understanding and application of the enzymatic reaction mechanism.
Numoto, N., Kamiya, N., Oda, M.(2023) bioRxiv
8IBM
Sulfate bound form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation
- PDB DOI: https://doi.org/10.2210/pdb8IBM/pdb
- Classification: HYDROLASE
- Organism(s): Saccharomonospora viridis
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2023-02-10 Released: 2023-03-15
- Funding Organization(s): Japan Society for the Promotion of Science (JSPS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.267
- R-Value Work: 0.234
- R-Value Observed: 0.235
Starting Model: experimental
View more details
This is version 1.1 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Alpha/beta hydrolase family protein | 263 | Saccharomonospora viridis | Mutation(s): 8 Gene Names: Cut190, SAMN02982918_2340 EC: 3.1.1.74 |  | |
UniProt | |||||
Find proteins for W0TJ64 (Saccharomonospora viridis) Explore W0TJ64 Go to UniProtKB: W0TJ64 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | W0TJ64 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 (Subject of Investigation/LOI) Query on SO4 | D [auth A], F [auth B] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| CA Query on CA | C [auth A], E [auth B] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.267
- R-Value Work: 0.234
- R-Value Observed: 0.235
- Space Group: P 3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 83.755 | α = 90 |
| b = 83.755 | β = 90 |
| c = 64.752 | γ = 120 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data reduction |
| XSCALE | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2023-03-15 Deposition Author(s): Emori, M., Numoto, N., Kamiya, N., Oda, M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Japan Society for the Promotion of Science (JSPS) | Japan | -- |
Revision History (Full details and data files)
- Version 1.0: 2023-03-15
Type: Initial release - Version 1.1: 2024-10-23
Changes: Data collection, Structure summary
