Download MendeleySolution Structure of the Closed Form of a Peptidyl-Prolyl Isomerase Reveals the Mechanism of Protein Folding
Kozlov, G., Trempe, J.-F., Perreault, A., Wong, M., Denisov, A., Ghandi, S., Gehring, K., Ekiel, I.To be published.
1L1P
Solution Structure of the PPIase Domain from E. coli Trigger Factor
- PDB DOI: https://doi.org/10.2210/pdb1L1P/pdb
- BMRB: 5298
- Classification: ISOMERASE
- Organism(s): Escherichia coli
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2002-02-19 Released: 2003-06-24
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 60
- Conformers Submitted: 30
- Selection Criteria: structures with the lowest energy
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 |
| trigger factor | 106 | Escherichia coli | Mutation(s): 0 EC: 5.2.1.8 |  | |
UniProt | |||||
Find proteins for P0A850 (Escherichia coli (strain K12)) Explore P0A850 Go to UniProtKB: P0A850 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P0A850 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 60
- Conformers Submitted: 30
- Selection Criteria: structures with the lowest energy
Entry History
Deposition Data
- Released Date: 2003-06-24 Deposition Author(s): Kozlov, G., Trempe, J.-F., Perreault, A., Wong, M., Denisov, A., Ghandi, S., Gehring, K., Ekiel, I., Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)
Revision History (Full details and data files)
- Version 1.0: 2003-06-24
Type: Initial release - Version 1.1: 2008-04-28
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2022-02-23
Changes: Data collection, Database references, Derived calculations
