Download MendeleyYeast SH3 domain structural genomics
Kursula, P., Kursula, I., Lehmann, F., Song, Y.-H., Wilmanns, M.To be published.
1SSH
Crystal structure of the SH3 domain from a S. cerevisiae hypothetical 40.4 kDa protein in complex with a peptide
- PDB DOI: https://doi.org/10.2210/pdb1SSH/pdb
- Classification: CONTRACTILE PROTEIN
- Organism(s): Saccharomyces cerevisiae, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2004-03-24 Released: 2005-04-12
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 Å
- R-Value Free: 0.203
- R-Value Work: 0.163
- R-Value Observed: 0.165
wwPDB Validation 3D Report Full Report
This is version 1.4 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 |
| Hypothetical 40.4 kDa protein in PES4-HIS2 intergenic region | 60 | Saccharomyces cerevisiae | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for P43603 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P43603 Go to UniProtKB: P43603 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P43603 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by: Sequence | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| 12-mer peptide from Cytoskeleton assembly control protein SLA1 | 12 | N/A | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for P32790 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P32790 Go to UniProtKB: P32790 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P32790 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 Å
- R-Value Free: 0.203
- R-Value Work: 0.163
- R-Value Observed: 0.165
- Space Group: P 41 21 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 33.92 | α = 90 |
| b = 33.92 | β = 90 |
| c = 113.1 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MAR345 | data collection |
| XDS | data scaling |
| AMoRE | phasing |
Entry History
Deposition Data
- Released Date: 2005-04-12 Deposition Author(s): Kursula, P., Kursula, I., Lehmann, F., Song, Y.-H., Wilmanns, M.
Revision History (Full details and data files)
- Version 1.0: 2005-04-12
Type: Initial release - Version 1.1: 2008-04-29
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2017-10-11
Changes: Refinement description - Version 1.4: 2023-10-25
Changes: Data collection, Database references, Refinement description
