MolNFT v1 · #43089 · protein
Backbone 1H, 13C, and 15N chemical shift assignments for the first dsrbd of protein HYL1
2L2N: “Backbone 1H, 13C, and 15N chemical shift assignments for the first dsrbd of protein HYL1”. Solution nmr. MolNFT v1 #43089 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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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