Download MendeleyTwo crystal structures of tropomyosin C-terminal fragment 176-273: exposure of the hydrophobic core to the solvent destabilizes the tropomyosin molecule
Minakata, S., Nitanai, Y., Maeda, K., Oda, N., Wakabayashi, K., Maeda, Y.To be published.
2EFR
Crystal structure of the c-terminal tropomyosin fragment with N- and C-terminal extensions of the leucine zipper at 1.8 angstroms resolution
- PDB DOI: https://doi.org/10.2210/pdb2EFR/pdb
- Classification: CONTRACTILE PROTEIN
- Organism(s): Saccharomyces cerevisiae, Oryctolagus cuniculus
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2007-02-23 Released: 2008-03-04
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.316
- R-Value Work: 0.237
- R-Value Observed: 0.237
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 |
| General control protein GCN4 and Tropomyosin 1 alpha chain | 155 | Saccharomyces cerevisiae, Oryctolagus cuniculus This entity is chimeric | Mutation(s): 1 |  | |
UniProt | |||||
Find proteins for P03069 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P03069 Go to UniProtKB: P03069 | |||||
Find proteins for P58772 (Oryctolagus cuniculus) Explore P58772 Go to UniProtKB: P58772 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Groups | P03069P58772 | ||||
Sequence AnnotationsExpand | |||||
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Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.316
- R-Value Work: 0.237
- R-Value Observed: 0.237
- Space Group: P 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 42.363 | α = 66.4 |
| b = 65.84 | β = 89.93 |
| c = 71.135 | γ = 90.03 |
| Software Name | Purpose |
|---|---|
| PHASER | phasing |
| CNS | refinement |
| HKL-2000 | data collection |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2008-03-04 Deposition Author(s): Minakata, S., Nitanai, Y., Maeda, K., Oda, N., Wakabayashi, K., Maeda, Y.
Revision History (Full details and data files)
- Version 1.0: 2008-03-04
Type: Initial release - Version 1.1: 2011-07-13
Changes: Derived calculations, Version format compliance - Version 1.2: 2017-08-23
Changes: Refinement description, Source and taxonomy - Version 1.3: 2021-11-10
Changes: Database references
