Download MendeleyStructural and further functional characterisation of a glycoside hydrolase family 3 beta-xylosidase from Thermotoga maritima
Gloster, T.M., Foltanyi, F., Hobbs, E.M., Pritchard, L.To be published.
7ZDY
Crystal structure of beta-xylosidase from Thermotoga maritima in complex with methyl-beta-D-xylopyranoside
- PDB DOI: https://doi.org/10.2210/pdb7ZDY/pdb
- Classification: HYDROLASE
- Organism(s): Thermotoga maritima MSB8
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2022-03-30 Released: 2023-04-19
- Funding Organization(s): Other government
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.46 Å
- R-Value Free: 0.191
- R-Value Work: 0.172
Starting Models: experimental
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This is version 1.1 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Beta-xylosidase | A [auth W], B [auth Y] | 801 | Thermotoga maritima MSB8 | Mutation(s): 0 Gene Names: Tmari_0073 EC: 3.2.1.37 (PDB Primary Data), 3.2.1.21 (UniProt) |  |
UniProt | |||||
Find proteins for Q9WXT1 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)) Explore Q9WXT1 Go to UniProtKB: Q9WXT1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9WXT1 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 6MJ (Subject of Investigation/LOI) Query on 6MJ | E [auth W], H [auth Y] | methyl beta-D-xylopyranoside C6 H12 O5 ZBDGHWFPLXXWRD-JGWLITMVSA-N |  | ||
| MPD Query on MPD | C [auth W], D [auth W], F [auth Y], G [auth Y] | (4S)-2-METHYL-2,4-PENTANEDIOL C6 H14 O2 SVTBMSDMJJWYQN-YFKPBYRVSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.46 Å
- R-Value Free: 0.191
- R-Value Work: 0.172
- Space Group: P 21 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 178.62 | α = 90 |
| b = 97.68 | β = 90 |
| c = 100.69 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| XSCALE | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2023-04-19 Deposition Author(s): Gloster, T.M., Foltanyi, F.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Other government | -- |
Revision History (Full details and data files)
- Version 1.0: 2023-04-19
Type: Initial release - Version 1.1: 2024-02-07
Changes: Data collection, Refinement description
