Research workbench
Solution structure of the knotted tudor domain of the yeast histone acetyltransferase, ESA1
Analyse Solution structure of the knotted tudor domain of the yeast histone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RO0
- Type
- protein
- Length
- 92 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase ESA1
- EC
- 2.3.1.48
- UniProt
- Q08649
Structure
solution nmr · 1 distinct chain · 3% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase ESA1 (EC 2.3.1.48) | protein | 92 | 3% helix, 38% strand | Q08649 |
Compared structures
- 2RO0 · Solution structure of the knotted tudor domain of the yeast histone acetyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q08649 · AlphaFold monomer V2.0 prediction for histone acetyltransferase ESA1 (Q08649) · a predicted model of the same protein · chain A against A, TM-score 0.79
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 Q08649
- Elsewhere: RCSB PDB 2RO0 · PDBe 2RO0 · UniProt Q08649
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