Research workbench
AlphaFold monomer V2.0 prediction for ig mu chain C region membrane- bound form (P04221)
Analyse AlphaFold monomer V2.0 prediction for ig mu chain C region membrane- bound form… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P04221
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Ig mu chain C region membrane-bound form
- UniProt
- P04221
- Pockets
- 3 · best druggability 0.52
Structure
1 distinct chain · 15% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ig mu chain C region membrane-bound form | protein | 479 | 15% helix, 46% strand | P04221 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.52 | 0.76 | 28 | empty |
| 2 | 162 | 0.43 | 0.75 | 25 | empty |
| 3 | 77 | 0.42 | 0.80 | 17 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 P04221
- Elsewhere: UniProt P04221 · AlphaFold DB P04221
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