Research workbench
AlphaFold monomer V2.0 prediction for methyl-cpg-binding domain protein 1 (Q9Z2E2)
Analyse AlphaFold monomer V2.0 prediction for methyl-cpg-binding domain protein 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9Z2E2
- Type
- protein
- Length
- 636 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1647F35A28688000958944B2f9d235C7c91d22B9
- Molecule
- Methyl-cpg-binding domain protein 1
- UniProt
- Q9Z2E2
- Pockets
- 3 · best druggability 0.58
Structure
1 distinct chain · 15% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-cpg-binding domain protein 1 | protein | 636 | 15% helix, 3% strand | Q9Z2E2 |
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 | 290 | 0.58 | 0.77 | 30 | empty |
| 2 | 215 | 0.45 | 0.73 | 26 | empty |
| 3 | 58 | 0.35 | 0.78 | 12 | empty |
Modifications
Observed in the structure: 1 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 Q9Z2E2
- Elsewhere: UniProt Q9Z2E2 · AlphaFold DB Q9Z2E2
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