Research workbench
The solution structure of the domain from MECP2 that binds to methylated DNA
Analyse The solution structure of the domain from MECP2 that binds to methylated DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QK9
- Type
- protein
- Length
- 92 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyl-cpg-binding protein 2
- UniProt
- P51608
- Pockets
- 1 · best druggability 0.47
Structure
solution nmr · 1 distinct chain · 15% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyl-cpg-binding protein 2 | protein | 92 | 15% helix, 14% strand | P51608 |
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 | 63 | 0.47 | 0.84 | 18 | empty |
Compared structures
- 1QK9 · The solution structure of the domain from MeCP2 that binds to methylated DNA · the same entry in another collection · chain A against A, TM-score 1.00
- P51608 · AlphaFold monomer V2.0 prediction for methyl-cpg-binding protein 2 (P51608) · a predicted model of the same protein · chain A against A, TM-score 0.69
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 P51608
- Elsewhere: RCSB PDB 1QK9 · PDBe 1QK9 · UniProt P51608
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