Research workbench
Solution structure of the tudor domain from mouse hypothetical protein homologous to histone acetyltransferase
Analyse Solution structure of the tudor domain from mouse hypothetical protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WGS
- Type
- protein
- Length
- 133 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myst histone acetyltransferase 1
- EC
- 2.3.1.48
- UniProt
- Q9D1P2
Structure
solution nmr · 1 distinct chain · 0% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myst histone acetyltransferase 1 (EC 2.3.1.48) | protein | 133 | 0% helix, 22% strand | Q9D1P2 |
Compared structures
- 1WGS · Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9D1P2 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT8 (Q9D1P2) · a predicted model of the same protein · chain A against A, TM-score 0.46
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 Q9D1P2
- Elsewhere: RCSB PDB 1WGS · PDBe 1WGS · UniProt Q9D1P2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.