Research workbench
Solution structure of the mynd domain from AML1-eto complexed with smrt, a corepressor
Analyse Solution structure of the mynd domain from AML1-eto complexed with smrt, a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ODD
- Type
- protein
- Length
- 63 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Smrt; Protein CBFA2T1
- UniProt
- Q06455
- Ligands
- ZN
Structure
solution nmr · 2 distinct chains · 17% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Smrt | protein | 13 | 0% helix, 23% strand | — |
| A | Protein CBFA2T1 | protein | 50 | 22% helix, 10% strand | Q06455 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–A · 546 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2ODD · Solution structure of the MYND domain from AML1-ETO complexed with SMRT, a corepressor · the same entry in another collection · chain B against B, TM-score 1.00
- Q06455 · AlphaFold monomer V2.0 prediction for protein CBFA2T1 (Q06455) · a predicted model of the same protein · chain A against A, TM-score 0.74
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 Q06455
- Elsewhere: RCSB PDB 2ODD · PDBe 2ODD · UniProt Q06455
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