Download MendeleyCrystal structure of the GH26 domain from PbGH26-GH5A endo-beta-mannanase/endo-beta-glucanase from Prevotella bryantii
McGregor, N.To be published.
6D2X
Crystal structure of the GH26 domain from PbGH26-GH5A endo-beta-mannanase/endo-beta-glucanase from Prevotella bryantii
- PDB DOI: https://doi.org/10.2210/pdb6D2X/pdb
- Classification: HYDROLASE
- Organism(s): Segatella baroniae B14
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2018-04-14 Released: 2019-10-16
- Funding Organization(s): Natural Sciences and Engineering Research Council (NSERC, Canada)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.72 Å
- R-Value Free: 0.196
- R-Value Work: 0.153
- R-Value Observed: 0.155
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| Aryl-phospho-beta-D-glucosidase BglC, GH1 family | 337 | Segatella baroniae B14 | Mutation(s): 0 Gene Names: PBR_0368, SAMN05444375_1266 |  | |
UniProt | |||||
Find proteins for D8DY19 (Segatella baroniae B14) Explore D8DY19 Go to UniProtKB: D8DY19 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | D8DY19 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PE3 Query on PE3 | C [auth A], D [auth A], E [auth A], F [auth A], G [auth A] | 3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL C28 H58 O15 ILLKMACMBHTSHP-UHFFFAOYSA-N |  | ||
| SO4 Query on SO4 | H [auth A], I [auth A], J [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | B [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.72 Å
- R-Value Free: 0.196
- R-Value Work: 0.153
- R-Value Observed: 0.155
- Space Group: P 32 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 73.577 | α = 90 |
| b = 73.577 | β = 90 |
| c = 105.086 | γ = 120 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| PHENIX | phasing |
| PHENIX | model building |
| Coot | model building |
Entry History & Funding Information
Deposition Data
- Released Date: 2019-10-16 Deposition Author(s): Stogios, P.J., Skarina, T., McGregor, N., Di Leo, R., Brumer, H., Savchenko, A.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Natural Sciences and Engineering Research Council (NSERC, Canada) | Canada | Industrial Biocatalysis Network |
Revision History (Full details and data files)
- Version 1.0: 2019-10-16
Type: Initial release - Version 1.1: 2020-01-08
Changes: Author supporting evidence - Version 1.2: 2023-10-04
Changes: Data collection, Database references, Refinement description
