Download MendeleySolution structure of the C-terminal SAM-domain of EphaA2: Ephrin type-A receptor 2 precursor (EC 2.7.10.1)
Goroncy, A.K., Sato, M., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S.To be published.
2E8N
Solution structure of the C-terminal SAM-domain of EphaA2: Ephrin type-A receptor 2 precursor (EC 2.7.10.1)
- PDB DOI: https://doi.org/10.2210/pdb2E8N/pdb
- Classification: TRANSFERASE, SIGNALING PROTEIN
- Organism(s): Homo sapiens
- Mutation(s): Yes
- Deposited: 2007-01-22 Released: 2008-01-29
Experimental Data Snapshot
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: structures with the least restraint violations
wwPDB Validation 3D Report Full Report
This is version 1.2 of the entry. See complete history.
Literature
To be published.
Macromolecules
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(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Ephrin type-A receptor 2 | 88 | Homo sapiens | Mutation(s): 1 Gene Names: EPHA2 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 | |||||
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Experimental Data & Validation
Experimental Data
- Method: SOLUTION NMR
- Conformers Calculated: 100
- Conformers Submitted: 20
- Selection Criteria: structures with the least restraint violations
Entry History
Deposition Data
- Released Date: 2008-01-29 Deposition Author(s): Goroncy, A.K., Sato, M., Koshiba, S., Inoue, M., Kigawa, T., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Revision History (Full details and data files)
- Version 1.0: 2008-01-29
Type: Initial release - Version 1.1: 2011-07-13
Changes: Version format compliance - Version 1.2: 2021-11-10
Changes: Data collection, Database references, Derived calculations
