Research workbench
AlphaFold monomer V2.0 prediction for ephrin type-B receptor 2 (P29323)
Analyse AlphaFold monomer V2.0 prediction for ephrin type-B receptor 2 (P29323) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P29323
- Type
- protein
- Length
- 1,055 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbbF4C29C4CA5f69fa0b37dDd9EcF5f8213FF5778
- UniProt
- P29323
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1055 | — | P29323 |
Compared structures
- 3ZFM · Crystal structure of EphB2 · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 3ZFM · Crystal structure of EPHB2 · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 2QBX · EphB2/SNEW Antagonistic Peptide Complex · an experimental structure of the same protein · chain A against A, TM-score 0.16
- 2QBX · EPHB2/SNEW antagonistic peptide complex · an experimental structure of the same protein · chain A against A, TM-score 0.16
- 1B4F · Oligomeric structure of the human EPHB2 receptor SAM domain · an experimental structure of the same protein · chain A against A, TM-score 0.07
- 1B4F · Oligomeric structure of the human EPHB2 receptor SAM domain · an experimental structure of the same protein · chain A against A, TM-score 0.07
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P29323
- Elsewhere: UniProt P29323 · AlphaFold DB P29323
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