Download MendeleyCrystal structure of dimeric ferredoxin-like protein (NP_888056.1) from Bordetella bronchiseptica at 1.90 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
2QYC
Crystal structure of a dimeric ferredoxin-like protein (bb1511) from bordetella bronchiseptica rb50 at 1.90 A resolution
- PDB DOI: https://doi.org/10.2210/pdb2QYC/pdb
- Classification: UNKNOWN FUNCTION
- Organism(s): Bordetella bronchiseptica RB50
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2007-08-14 Released: 2007-08-28
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.236
- R-Value Work: 0.177
- R-Value Observed: 0.180
wwPDB Validation 3D Report Full Report
This is version 1.4 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 |
| Ferredoxin-like protein | 103 | Bordetella bronchiseptica RB50 | Mutation(s): 0 Gene Names: NP_888056.1, BB1511 |  | |
UniProt | |||||
Find proteins for A0A0H3LJT0 (Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)) Explore A0A0H3LJT0 Go to UniProtKB: A0A0H3LJT0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A0A0H3LJT0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | C [auth A], D [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | F [auth B] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| CL Query on CL | E [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.90 Å
- R-Value Free: 0.236
- R-Value Work: 0.177
- R-Value Observed: 0.180
- Space Group: P 32 2 1
- Diffraction Data: https://doi.org/10.18430/M32QYC
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 50.82 | α = 90 |
| b = 50.82 | β = 90 |
| c = 142.17 | γ = 120 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SOLVE | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| XDS | data reduction |
Entry History
Deposition Data
- Released Date: 2007-08-28 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2007-08-28
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-10-25
Changes: Author supporting evidence, Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-01-25
Changes: Database references, Derived calculations
