MolNFT v1 · #43087 · protein
Solution structure of the coiled-coil complex between MBD2 and P66ALPHA
2L2L · Transcriptional repressor P66-alpha: “Solution structure of the coiled-coil complex between MBD2 and P66ALPHA”. Solution nmr. MolNFT v1 #43087 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2L2L
- Type
- protein
- Length
- 79 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional repressor P66-alpha; Methyl-cpg-binding domain protein 2
- UniProt
- Q86YP4, Q9UBB5
Structure
solution nmr · 2 distinct chains · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional repressor P66-alpha | protein | 43 | 72% helix, 0% strand | Q86YP4 |
| B | Methyl-cpg-binding domain protein 2 | protein | 36 | 64% helix, 0% strand | Q9UBB5 |
Interfaces
1 interface between chains.
- A–B · 705 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2L2L · Solution structure of the coiled-coil complex between MBD2 and p66alpha · the same entry in another collection · chain A against A, TM-score 1.00
- Q86YP4 · AlphaFold monomer V2.0 prediction for transcriptional repressor P66-alpha (Q86YP4) · a predicted model of the same protein · chain A against A, TM-score 0.72
- Q9UBB5 · AlphaFold monomer V2.0 prediction for methyl-cpg-binding domain protein 2 (Q9UBB5) · a predicted model of the same protein · chain B against A, TM-score 0.72
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 Q86YP4
- Every structure of UniProt Q9UBB5
- Elsewhere: RCSB PDB 2L2L · PDBe 2L2L · UniProt Q86YP4 · UniProt Q9UBB5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.