Research workbench
Structure of arabidopsis HYL1 and its molecular implications for miRNA processing
Analyse Structure of arabidopsis HYL1 and its molecular implications for miRNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ADG
- Type
- protein
- Length
- 72 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F21M12.9 protein
- UniProt
- O04492
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F21M12.9 protein | protein | 72 | 38% helix, 28% strand | O04492 |
Compared structures
- 3ADG · Structure of Arabidopsis HYL1 and its molecular implications for miRNA processing · the same entry in another collection · chain A against A, TM-score 1.00
- O04492 · AlphaFold monomer V2.0 prediction for double-stranded RNA-binding protein 1 (O04492) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 O04492
- Elsewhere: RCSB PDB 3ADG · PDBe 3ADG · UniProt O04492
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