Download MendeleyStructure of the leucine-rich repeat domain of the type III effector XCV3220 (XopL)
Singer, A.U., Schulze, S., Xu, X., Skarina, T., Cui, H., Egler, M., Srikumar, T., Raught, B., Savchenko, A., Bonas, U.To be published.
4FCG
Structure of the leucine-rich repeat domain of the type III effector XCV3220 (XopL)
- PDB DOI: https://doi.org/10.2210/pdb4FCG/pdb
- Classification: Structural Genomics, Unknown Function
- Organism(s): Xanthomonas euvesicatoria pv. vesicatoria str. 85-10
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2012-05-24 Released: 2012-06-13
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.226
- R-Value Work: 0.171
- R-Value Observed: 0.174
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 |
| uncharacterized protein | 328 | Xanthomonas euvesicatoria pv. vesicatoria str. 85-10 | Mutation(s): 0 Gene Names: XCV3220 |  | |
UniProt | |||||
Find proteins for Q3BQL2 (Xanthomonas campestris pv. vesicatoria (strain 85-10)) Explore Q3BQL2 Go to UniProtKB: Q3BQL2 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q3BQL2 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PO4 Query on PO4 | F [auth A], G [auth A], H [auth A] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |  | ||
| EDO Query on EDO | I [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| CL Query on CL | B [auth A], C [auth A], D [auth A], E [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.00 Å
- R-Value Free: 0.226
- R-Value Work: 0.171
- R-Value Observed: 0.174
- Space Group: C 2 2 21
- Diffraction Data: https://doi.org/10.18430/M34FCG
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 50.463 | α = 90 |
| b = 95.228 | β = 90 |
| c = 115.465 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-3000 | data collection |
| SHELXCD | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
Entry History
Deposition Data
- Released Date: 2012-06-13 Deposition Author(s): Singer, A.U., Xu, X., Cui, H., Zimmerman, M.D., Minor, W., Joachimiak, A., Savchenko, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2012-06-13
Type: Initial release - Version 1.1: 2017-10-25
Changes: Author supporting evidence, Refinement description - Version 1.2: 2022-04-13
Changes: Database references, Derived calculations, Structure summary
