Download MendeleyDivergence of PUF protein specificity through variations in an RNA-binding pocket
Qiu, C., Kershner, A., Wang, Y., Holley, C.H., Wilinski, D., Keles, S., Kimble, J., Wickens, M., Hall, T.M.T.(2012) J Biol Chem
3V71
Crystal structure of PUF-6 in complex with 5BE13 RNA
- PDB DOI: https://doi.org/10.2210/pdb3V71/pdb
- NAKB: 3V71
- Classification: RNA binding protein/RNA
- Organism(s): Caenorhabditis elegans
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2011-12-20 Released: 2012-01-04
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.90 Å
- R-Value Free: 0.241
- R-Value Work: 0.207
- R-Value Observed: 0.209
wwPDB Validation 3D Report Full Report
This is version 1.1 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Puf (Pumilio/fbf) domain-containing protein 7, confirmed by transcript evidence | 382 | Caenorhabditis elegans | Mutation(s): 0 Gene Names: puf-7, B0273.2 |  | |
UniProt | |||||
Find proteins for O44169 (Caenorhabditis elegans) Explore O44169 Go to UniProtKB: O44169 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O44169 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar nucleic acids by: Sequence | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Length | Organism | Image | |
| RNA (5'-R(*CP*UP*CP*UP*GP*UP*AP*UP*CP*UP*UP*GP*U)-3') | 13 | Caenorhabditis elegans |  | ||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| EPE Query on EPE | C [auth B] | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID C8 H18 N2 O4 S JKMHFZQWWAIEOD-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.90 Å
- R-Value Free: 0.241
- R-Value Work: 0.207
- R-Value Observed: 0.209
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 67.806 | α = 90 |
| b = 87.836 | β = 90 |
| c = 129.782 | γ = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| PHASER | phasing |
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2012-01-04 Deposition Author(s): Qiu, C., Kershner, A., Wang, Y., Holley, C.H., Wilinski, D., Keles, S., Kimble, J., Wickens, M., Hall, T.M.T.
Revision History (Full details and data files)
- Version 1.0: 2012-01-04
Type: Initial release - Version 1.1: 2023-09-13
Changes: Data collection, Database references, Derived calculations, Refinement description
