Download MendeleyX-ray crystal structure of putative HTH transcription regulator from Archaeoglobus fulgidus
Osipiuk, J., Skarina, T., Savchenko, A., Edwards, A., Cymborowski, M., Minor, W., Joachimiak, A.To be published.
1SFX
X-ray crystal structure of putative HTH transcription regulator from Archaeoglobus fulgidus
- PDB DOI: https://doi.org/10.2210/pdb1SFX/pdb
- Classification: structural genomics, unknown function
- Organism(s): Archaeoglobus fulgidus DSM 4304
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2004-02-20 Released: 2004-08-03
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.55 Å
- R-Value Free: 0.183
- R-Value Work: 0.148
- R-Value Observed: 0.150
wwPDB Validation 3D Report Full Report
This is version 1.3 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 |
| Conserved hypothetical protein AF2008 | 109 | Archaeoglobus fulgidus DSM 4304 | Mutation(s): 3 Gene Names: AF2008 |  | |
UniProt | |||||
Find proteins for O28271 (Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)) Explore O28271 Go to UniProtKB: O28271 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O28271 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EDO Query on EDO | E [auth A], F [auth A], H [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| CL Query on CL | C [auth A], D [auth A], G [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: 1.55 Å
- R-Value Free: 0.183
- R-Value Work: 0.148
- R-Value Observed: 0.150
- Space Group: C 1 2 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 64.265 | α = 90 |
| b = 59.634 | β = 90.11 |
| c = 63.498 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data reduction |
| SCALEPACK | data scaling |
| SHELXD | phasing |
| SOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2004-08-03 Deposition Author(s): Osipiuk, J., Skarina, T., Savchenko, A., Edwards, A., Cymborowski, M., Minor, W., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2004-08-03
Type: Initial release - Version 1.1: 2008-04-29
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Source and taxonomy, Version format compliance - Version 1.3: 2022-04-13
Changes: Database references, Derived calculations, Structure summary
