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 | pdb_00002kym
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 1.3 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 |
| 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 EC: 2.7.11.1 |  | |
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 | |||||
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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 - Version 1.3: 2024-05-01
Changes: Data collection, Database references
