Research workbench
AlphaFold monomer V2.0 prediction for ephrin-B1 (P52795)
Analyse AlphaFold monomer V2.0 prediction for ephrin-B1 (P52795) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P52795
- Type
- protein
- Length
- 345 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB74A3a10Bdfe3C1226B2CF28959A9C5F69dc531D
- Molecule
- Ephrin-B1
- UniProt
- P52795
- Pockets
- 1 · best druggability 0.40
Structure
1 distinct chain · 21% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ephrin-B1 | protein | 345 | 21% helix, 14% strand | P52795 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.40 | 0.80 | 15 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6P7S · Crystal structure of the cedar henipavirus attachment G glycoprotein globular domain in… · an experimental structure of the same protein · chain A against B, TM-score 0.39
- 6P7S · Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein globular domain in… · an experimental structure of the same protein · chain A against B, TM-score 0.39
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 P52795
- Elsewhere: UniProt P52795 · AlphaFold DB P52795
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