Download MendeleyThe crystal structure of an aerotolerance-related membrane protein from Bacteroides fragilis NCTC 9343 with multiple mutations to serines.
Fan, Y., Tan, K., Bigelow, L., Bearden, J., Joachimiak, A.To be published.
4JDU
The crystal structure of an aerotolerance-related membrane protein from Bacteroides fragilis NCTC 9343 with multiple mutations to serines.
- PDB DOI: https://doi.org/10.2210/pdb4JDU/pdb
- Classification: MEMBRANE PROTEIN
- Organism(s): Bacteroides fragilis NCTC 9343
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2013-02-25 Released: 2013-03-27
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.47 Å
- R-Value Free: 0.198
- R-Value Work: 0.182
- R-Value Observed: 0.182
wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| Aerotolerance-related membrane protein | 215 | Bacteroides fragilis NCTC 9343 | Mutation(s): 6 Gene Names: batB, BF2500, BF9343_2419 |  | |
UniProt | |||||
Find proteins for Q5LCG5 (Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow)) Explore Q5LCG5 Go to UniProtKB: Q5LCG5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q5LCG5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| FMT Query on FMT | B [auth A] | FORMIC ACID C H2 O2 BDAGIHXWWSANSR-UHFFFAOYSA-N |  | ||
| CA Query on CA | C [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
| Modified Residues 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MLY Query on MLY | A | L-PEPTIDE LINKING | C8 H18 N2 O2 |  | LYS |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.47 Å
- R-Value Free: 0.198
- R-Value Work: 0.182
- R-Value Observed: 0.182
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 39.277 | α = 90 |
| b = 49.871 | β = 90 |
| c = 85.451 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| SHELXD | phasing |
| MLPHARE | phasing |
| DM | model building |
| ARP | model building |
| WARP | model building |
| HKL-3000 | phasing |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| DM | phasing |
Entry History
Deposition Data
- Released Date: 2013-03-27 Deposition Author(s): Fan, Y., Tan, K., Bigelow, L., Bearden, J., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2013-03-27
Type: Initial release
