Download MendeleyStructural basis for mucin-type O-glycan recognition by proteins of a Bacteroides thetaiotaomicron polysaccharide utilization loci
Costa, R.L., Correia, V.G.To be published.
7BLH
Structure of CBM BT3015C from Bacteroides thetaiotaomicron in complex with O-GalNAc core 1-Thr
- PDB DOI: https://doi.org/10.2210/pdb7BLH/pdb
- Classification: SUGAR BINDING PROTEIN
- Organism(s): Bacteroides thetaiotaomicron VPI-5482
- Expression System: Escherichia coli 'BL21-Gold(DE3)pLysS AG
- Mutation(s): No
- Deposited: 2021-01-18 Released: 2022-03-02
- Funding Organization(s): Foundation for Science and Technology (FCT)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.79 ?
- R-Value Free: 0.203
- R-Value Work: 0.157
- R-Value Observed: 0.159
Starting Model: 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 |
| family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron | A [auth AAAA] | 162 | Bacteroides thetaiotaomicron VPI-5482 | Mutation(s): 0 Gene Names: BT_3015 |  |
UniProt | |||||
Find proteins for Q8A3D9 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8A3D9 Go to UniProtKB: Q8A3D9 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8A3D9 | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| THR (Subject of Investigation/LOI) Query on THR | C [auth AAAA] | THREONINE C4 H9 N O3 AYFVYJQAPQTCCC-GBXIJSLDSA-N |  | ||
| CA Query on CA | D [auth AAAA] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.79 ?
- R-Value Free: 0.203
- R-Value Work: 0.157
- R-Value Observed: 0.159
- Space Group: P 21 21 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 35.525 | ¦Á = 90 |
| b = 64.011 | ¦Â = 90 |
| c = 70.211 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| PHENIX | refinement |
| SADABS | data reduction |
| SAINT | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2022-03-02 Deposition Author(s): Costa, R.L., Carvalho, A.L.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Foundation for Science and Technology (FCT) | Portugal | PTDC/BIA-MIB/31730/2017 |
Revision History (Full details and data files)
- Version 1.0: 2022-03-02
Type: Initial release - Version 1.1: 2024-01-31
Changes: Data collection, Refinement description
