Download MendeleyCrystal Structure of PRC-barrel Domain Protein from Rhodopseudomonas palustris
Kim, Y., Tesar, C., Jedrzejczak, R., Kinney, J., Babnigg, G., Harwood, C., Kerfeld, C., Joachimiak, A.To be published.
3HTR
Crystal Structure of PRC-barrel Domain Protein from Rhodopseudomonas palustris
- PDB DOI: https://doi.org/10.2210/pdb3HTR/pdb
- Classification: structural genomics, unknown function
- Organism(s): Rhodopseudomonas palustris
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2009-06-12 Released: 2009-07-07
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.06 Å
- R-Value Free: 0.231
- R-Value Work: 0.193
- R-Value Observed: 0.197
wwPDB Validation 3D Report Full Report
This is version 1.1 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 PRC-barrel Domain Protein | 120 | Rhodopseudomonas palustris | Mutation(s): 0 Gene Names: RPA4758 |  | |
UniProt | |||||
Find proteins for Q6N0K4 (Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)) Explore Q6N0K4 Go to UniProtKB: Q6N0K4 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q6N0K4 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ZN Query on ZN | C [auth A], D [auth A], G [auth B], H [auth B] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| ACY Query on ACY | E [auth A], F [auth A], I [auth B] | ACETIC ACID C2 H4 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-N |  | ||
| 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: 2.06 Å
- R-Value Free: 0.231
- R-Value Work: 0.193
- R-Value Observed: 0.197
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 25.644 | α = 90 |
| b = 63.061 | β = 99.39 |
| c = 61.866 | γ = 90 |
| Software Name | Purpose |
|---|---|
| SBC-Collect | data collection |
| HKL-3000 | data collection |
| PHENIX | model building |
| SOLVE | phasing |
| RESOLVE | model building |
| Coot | model building |
| PHENIX | refinement |
| HKL-3000 | data reduction |
| HKL-3000 | data scaling |
| PHENIX | phasing |
| RESOLVE | phasing |
Entry History
Deposition Data
- Released Date: 2009-07-07 Deposition Author(s): Kim, Y., Tesar, C., Jedrzejczak, R., Kinney, J., Babnigg, G., Harwood, C., Kerfeld, C., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-07-07
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance
