Research workbench
AlphaFold monomer V2.0 prediction for ephrin-A1 (P20827)
Analyse AlphaFold monomer V2.0 prediction for ephrin-A1 (P20827) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P20827
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa130963659F9ADED1C735201Bb05F57675e205B8
- UniProt
- P20827
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 205 | — | P20827 |
Compared structures
- 3HEI · Ligand Recognition by A-Class Eph Receptors: Crystal Structures of the EphA2… · an experimental structure of the same protein · chain A against L, TM-score 0.63
- 3HEI · Ligand recognition by a-class eph receptors: crystal structures of the EPHA2… · an experimental structure of the same protein · chain A against L, TM-score 0.63
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 P20827
- Elsewhere: UniProt P20827 · AlphaFold DB P20827
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