Download MendeleyIn situ cryo-ET visualization of mitochondrial depolarization and mitophagic engulfment
Rose, K.M., Herrmann, E., Kakudji, E., Lizarrondo, J., Celebi, A.Y., Wilfling, F., Lewis, S.C., Hurley, J.H.To be published.
9O6S | pdb_00009o6s
Structure of the human prohibitin complex in the closed state
- PDB DOI: https://doi.org/10.2210/pdb9O6S/pdb
- EM Map EMD-70179: EMDB EMDataResource
- Classification: MEMBRANE PROTEIN
- Organism(s): Homo sapiens
- Mutation(s): No
- Deposited: 2025-04-14 Released: 2025-05-07
- Funding Organization(s): Aligning Science Across Parkinsons (ASAP), Alexander von Humboldt Foundation, National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: ELECTRON MICROSCOPY
- Resolution: 21.0 Å
- Aggregation State: CELL
- Reconstruction Method: SUBTOMOGRAM AVERAGING
Starting Model: in silico
View more details
wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| Prohibitin-2 | 299 | Homo sapiens | Mutation(s): 0 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q99623 (Homo sapiens) Explore Q99623 Go to UniProtKB: Q99623 | |||||
PHAROS: Q99623 GTEx: ENSG00000215021 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q99623 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Prohibitin 1 | 272 | Homo sapiens | Mutation(s): 0 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P35232 (Homo sapiens) Explore P35232 Go to UniProtKB: P35232 | |||||
PHAROS: P35232 GTEx: ENSG00000167085 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P35232 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: ELECTRON MICROSCOPY
- Resolution: 21.0 Å
- Aggregation State: CELL
- Reconstruction Method: SUBTOMOGRAM AVERAGING
| Task | Software Package | Version |
|---|---|---|
| MODEL REFINEMENT | PHENIX | |
| RECONSTRUCTION | RELION | 5.0 |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-05-07 Deposition Author(s): Rose, K., Herrmann, E., Hurley, J.H.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Aligning Science Across Parkinsons (ASAP) | United States | ASAP-000350 |
| Alexander von Humboldt Foundation | Germany | -- |
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | U24 GM139168 |
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | U24 GM139166 |
Revision History (Full details and data files)
- Version 1.0: 2025-05-07
Type: Initial release
