Download MendeleyStructure and function of the EphA2:SHIP2 SAM domain heterodimer
Lee, H., Hota, P., Preeti, C., Wang, B., Buck, M.To be published.
2KSO | pdb_00002kso
EphA2:SHIP2 SAM:SAM complex
- PDB DOI: https://doi.org/10.2210/pdb2KSO/pdb
- Classification: PROTEIN BINDING
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2010-01-10 Released: 2011-07-27
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 15
- Selection Criteria: structures with the least restraint violations
wwPDB Validation 3D Report Full Report
This is version 1.1 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 |
| Ephrin type-A receptor 2 | 82 | Homo sapiens | Mutation(s): 0 Gene Names: EPHA2, ECK EC: 2.7.10.1 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P29317 (Homo sapiens) Explore P29317 Go to UniProtKB: P29317 | |||||
PHAROS: P29317 GTEx: ENSG00000142627 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P29317 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 | 76 | Homo sapiens | Mutation(s): 0 Gene Names: INPPL1, SHIP2 EC: 3.1.3.86 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for O15357 (Homo sapiens) Explore O15357 Go to UniProtKB: O15357 | |||||
PHAROS: O15357 GTEx: ENSG00000165458 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O15357 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 15
- Selection Criteria: structures with the least restraint violations
Entry History
Deposition Data
- Released Date: 2011-07-27 Deposition Author(s): Hota, P.K., Preeti, C., Stetzik, L., Kim, S., Wang, B., Lee, H., Buck, M.
Revision History (Full details and data files)
- Version 1.0: 2011-07-27
Type: Initial release - Version 1.1: 2024-05-01
Changes: Data collection, Database references
