Download MendeleyInhibition of protein-only RNase P with Gambogic acid and Juglone
Wu, N., Karasik, A., Muehlbauer, L., Koutmos, M., Fierke, C.A.To be published.
6BV5
Structure of proteinaceous RNase P 1 (PRORP1) from A. thaliana after 45-minute soak with juglone
- PDB DOI: https://doi.org/10.2210/pdb6BV5/pdb
- Classification: HYDROLASE/HYDROLASE INHIBITOR
- Organism(s): Arabidopsis thaliana
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2017-12-12 Released: 2019-06-12
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.79 Å
- R-Value Free: 0.223
- R-Value Work: 0.196
- R-Value Observed: 0.197
Starting Model: experimental
View more details
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 |
| Proteinaceous RNase P 1, chloroplastic/mitochondrial | 501 | Arabidopsis thaliana | Mutation(s): 0 Gene Names: PRORP1, At2g32230, F22D22.2 EC: 3.1.26.5 |  | |
UniProt | |||||
Find proteins for Q66GI4 (Arabidopsis thaliana) Explore Q66GI4 Go to UniProtKB: Q66GI4 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q66GI4 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| JUG Query on JUG | B [auth A] | 5-hydroxynaphthalene-1,4-dione C10 H6 O3 KQPYUDDGWXQXHS-UHFFFAOYSA-N |  | ||
| ZN Query on ZN | D [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| MN Query on MN | C [auth A] | MANGANESE (II) ION Mn WAEMQWOKJMHJLA-UHFFFAOYSA-N |  | ||
| CL Query on CL | E [auth A], F [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.79 Å
- R-Value Free: 0.223
- R-Value Work: 0.196
- R-Value Observed: 0.197
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 41.616 | α = 90 |
| b = 110.838 | β = 90 |
| c = 140.743 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2019-06-12 Deposition Author(s): Karasik, A., Wu, N., Fierke, C.A., Koutmos, M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | R01GM117141 |
Revision History (Full details and data files)
- Version 1.0: 2019-06-12
Type: Initial release - Version 1.1: 2020-01-01
Changes: Author supporting evidence - Version 1.2: 2023-10-04
Changes: Data collection, Database references, Derived calculations, Refinement description - Version 1.3: 2024-10-09
Changes: Structure summary
