Download MendeleyTHE CRYSTAL STRUCTURE OF THE W169Y MUTANT OF ALPHA-GLUCOSIDASE (GH 31) FROM RUMINOCOCCUS OBEUM ATCC 29174 in complex with miglitol
Tan, K., Tesar, C., Jedrzejczak, R., Joachimiak, A.To be published.
6CA3
THE CRYSTAL STRUCTURE OF THE W169Y MUTANT OF ALPHA-GLUCOSIDASE (GH 31) FROM RUMINOCOCCUS OBEUM ATCC 29174 in complex with miglitol
- PDB DOI: https://doi.org/10.2210/pdb6CA3/pdb
- Classification: HYDROLASE
- Organism(s): Blautia obeum ATCC 29174
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2018-01-29 Released: 2018-02-28
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.74 Å
- R-Value Free: 0.191
- R-Value Work: 0.153
- R-Value Observed: 0.155
Starting Model: experimental
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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 |
| Glycosyl hydrolase, family 31 | 666 | Blautia obeum ATCC 29174 | Mutation(s): 1 Gene Names: RUMOBE_03919 EC: 3.2.1 |  | |
UniProt | |||||
Find proteins for A5ZY13 (Blautia obeum ATCC 29174) Explore A5ZY13 Go to UniProtKB: A5ZY13 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A5ZY13 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| MIG Query on MIG | C [auth A], E [auth B] | (2R,3R,4R,5S)-1-(2-hydroxyethyl)-2-(hydroxymethyl)piperidine-3,4,5-triol C8 H17 N O5 IBAQFPQHRJAVAV-ULAWRXDQSA-N |  | ||
| GOL Query on GOL | D [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.74 Å
- R-Value Free: 0.191
- R-Value Work: 0.153
- R-Value Observed: 0.155
- Space Group: P 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 64.685 | α = 111.32 |
| b = 70.826 | β = 107.42 |
| c = 88.103 | γ = 97.66 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| HKL-3000 | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2018-02-28 Deposition Author(s): Tan, K., Tesar, C., Jedrzejczak, R., Joachimiak, A., Midwest Center for Macromolecular Research (MCMR)
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | GM094585 |
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | GM115586 |
Revision History (Full details and data files)
- Version 1.0: 2018-02-28
Type: Initial release - Version 1.1: 2021-07-21
Changes: Author supporting evidence - Version 1.2: 2023-10-04
Changes: Data collection, Database references, Refinement description
