Download MendeleySystematic Functional and Computational Analysis of Glucose-Binding Residues in Glycoside Hydrolase Family GH116.
Huang, M., Pengthaisong, S., Charoenwattanasatien, R., Thinkumrob, N., Jitonnom, J., Ketudat Cairns, J.R.(2022) Catalysts 12
7W2S
Crystal structure of TxGH116 E730A mutant from Thermoanaerobacterium xylanolyticum with glucose
- PDB DOI: https://doi.org/10.2210/pdb7W2S/pdb
- Classification: HYDROLASE
- Organism(s): Thermoanaerobacterium xylanolyticum LX-11
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2021-11-24 Released: 2022-04-06
- Funding Organization(s): Other government
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.193
- R-Value Work: 0.154
- R-Value Observed: 0.156
Starting Model: experimental
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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 |
| Glucosylceramidase | 842 | Thermoanaerobacterium xylanolyticum LX-11 | Mutation(s): 1 Gene Names: Thexy_2211 EC: 3.2.1.45 |  | |
UniProt | |||||
Find proteins for F6BL85 (Thermoanaerobacterium xylanolyticum (strain ATCC 49914 / DSM 7097 / LX-11)) Explore F6BL85 Go to UniProtKB: F6BL85 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | F6BL85 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| BGC (Subject of Investigation/LOI) Query on BGC | B [auth A] | beta-D-glucopyranose C6 H12 O6 WQZGKKKJIJFFOK-VFUOTHLCSA-N |  | ||
| GOL (Subject of Investigation/LOI) Query on GOL | C [auth A] D [auth A] E [auth A] F [auth A] G [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | L [auth A], M [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| CA Query on CA | N [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.85 Å
- R-Value Free: 0.193
- R-Value Work: 0.154
- R-Value Observed: 0.156
- Space Group: P 21 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 177.364 | α = 90 |
| b = 54.708 | β = 90 |
| c = 83.216 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
| PDB_EXTRACT | data extraction |
| Coot | model building |
Entry History & Funding Information
Deposition Data
- Released Date: 2022-04-06 Deposition Author(s): Huang, M., Pengthaisong, S., Charoenwattanasatien, R., Jitonnom, J., Ketudat Cairns, J.R.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Other government | Thailand | Suranaree University of Technology |
| Other government | Thailand | Thailand Research Fund |
| Other government | Thailand | Thailand Science Research and Innovation |
| Other government | Thailand | Synchrotron Light Research Institute (Public Organization) |
| Other government | Thailand | University of Phayao |
Revision History (Full details and data files)
- Version 1.0: 2022-04-06
Type: Initial release - Version 1.1: 2023-11-29
Changes: Data collection, Refinement description
