Research workbench
AlphaFold monomer V2.0 prediction for ephrin-B1 (P98172)
Analyse AlphaFold monomer V2.0 prediction for ephrin-B1 (P98172) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P98172
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- UniProt
- P98172
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 346 | — | P98172 |
Compared structures
- 6THG · Cedar virus attachment glycoprotein (G) in complex with human ephrin- B1 · an experimental structure of the same protein · chain A against F, TM-score 0.38
- 6THG · Cedar Virus attachment glycoprotein (G) in complex with human ephrin-B1 · an experimental structure of the same protein · chain A against F, TM-score 0.38
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 P98172
- Elsewhere: UniProt P98172 · AlphaFold DB P98172
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