Research workbench
Backbone 1H, 13C, and 15N chemical shift assignments for the first dsrbd of protein HYL1
Analyse Backbone 1H, 13C, and 15N chemical shift assignments for the first dsrbd of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L2N
- Type
- protein
- Length
- 71 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O04492
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 71 | — | O04492 |
Compared structures
- 2L2N · Backbone 1H, 13C, and 15N Chemical Shift Assignments for the first dsRBD of protein HYL1 · 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 0.91
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 2L2N · PDBe 2L2N · UniProt O04492
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