Download MendeleyStructural and functional characterization of an unusual SH3 domain from the fungal scaffold protein, Bem1p
Gorelik, M., Muhandiram, R., Yin, W., Davidson, A.R.To be published.
2KYM
Solution structure of the Bem1p SH3-CI domain from L.elongisporus in complex with Ste20p peptide
- PDB DOI: https://doi.org/10.2210/pdb2KYM/pdb
- BMRB: 16970
- Classification: SIGNALING PROTEIN
- Organism(s): Lodderomyces elongisporus NRRL YB-4239, Saccharomyces cerevisiae
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2010-06-02 Released: 2010-06-23
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: target function
wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| Bud emergence protein 1 | 120 | Lodderomyces elongisporus NRRL YB-4239 | Mutation(s): 0 Gene Names: LELG_04233 |  | |
UniProt | |||||
Find proteins for A5E3P5 (Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL YB-4239)) Explore A5E3P5 Go to UniProtKB: A5E3P5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | A5E3P5 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by: Sequence | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Peptide form Serine/threonine-protein kinase STE20 | 16 | Saccharomyces cerevisiae | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for Q03497 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore Q03497 Go to UniProtKB: Q03497 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q03497 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: target function
Entry History
Deposition Data
- Released Date: 2010-06-23 Deposition Author(s): Gorelik, M., Muhandiram, R., Davidson, A.R.
Revision History (Full details and data files)
- Version 1.0: 2010-06-23
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2020-02-05
Changes: Data collection, Database references, Other
