Research workbench
AlphaFold monomer V2.0 prediction for seh-associated protein 4 (P38164)
Analyse AlphaFold monomer V2.0 prediction for seh-associated protein 4 (P38164) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P38164
- Type
- protein
- Length
- 1,038 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Seh-associated protein 4
- UniProt
- P38164
- Pockets
- 16 · best druggability 0.77
Structure
1 distinct chain · 28% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Seh-associated protein 4 | protein | 1038 | 28% helix, 19% strand | P38164 |
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 518 | 0.77 | 0.85 | 53 | empty |
| 2 | 55 | 0.64 | 0.94 | 19 | empty |
| 3 | 367 | 0.59 | 0.76 | 43 | empty |
| 4 | 216 | 0.58 | 0.80 | 28 | empty |
| 5 | 250 | 0.55 | 0.78 | 28 | empty |
Compared structures
- 8ADL · Cryo-EM structure of the SEA complex · an experimental structure of the same protein · chain A against G, TM-score 0.57
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 P38164
- Elsewhere: UniProt P38164 · AlphaFold DB P38164
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