Download MendeleyCrystal structure of a leucine-rich repeat protein (BT_0210) from Bacteroides thetaiotaomicron VPI-5482 at 2.80 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
4ECN
Crystal structure of a leucine-rich repeat protein (BT_0210) from Bacteroides thetaiotaomicron VPI-5482 at 2.80 A resolution
- PDB DOI: https://doi.org/10.2210/pdb4ECN/pdb
- Classification: UNKNOWN FUNCTION
- Organism(s): Bacteroides thetaiotaomicron VPI-5482
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2012-03-26 Released: 2012-05-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.80 Å
- R-Value Free: 0.232
- R-Value Work: 0.182
- R-Value Observed: 0.184
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 |
| Leucine-rich repeat protein | 876 | Bacteroides thetaiotaomicron VPI-5482 | Mutation(s): 0 Gene Names: BT_0210 |  | |
UniProt | |||||
Find proteins for Q8ABA0 (Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)) Explore Q8ABA0 Go to UniProtKB: Q8ABA0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q8ABA0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CL Query on CL | C [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| NA Query on NA | B [auth A] | SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N |  | ||
| 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: 2.80 Å
- R-Value Free: 0.232
- R-Value Work: 0.182
- R-Value Observed: 0.184
- Space Group: P 21 21 21
- Diffraction Data: https://doi.org/10.18430/M34ECN
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 85.399 | α = 90 |
| b = 105.463 | β = 90 |
| c = 161.196 | γ = 90 |
| Software Name | Purpose |
|---|---|
| MolProbity | model building |
| PDB_EXTRACT | data extraction |
| SHELX | phasing |
| SHARP | phasing |
| XSCALE | data scaling |
| BUSTER-TNT | refinement |
| XDS | data reduction |
| SHELXD | phasing |
| BUSTER | refinement |
Entry History
Deposition Data
- Released Date: 2012-05-23 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2012-05-23
Type: Initial release - Version 1.1: 2017-11-15
Changes: Refinement description - Version 1.2: 2023-02-01
Changes: Database references, Derived calculations
