Research workbench
RNA structural dynamics are modulated through anti-folding by chaperones
Analyse RNA structural dynamics are modulated through anti-folding by chaperones in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LRX
- Type
- protein
- Length
- 45 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein stpa
- UniProt
- P0ACG1
Structure
solution nmr · 1 distinct chain · 24% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-binding protein stpa | protein | 45 | 24% helix, 4% strand | P0ACG1 |
Compared structures
- 2LRX · RNA structural dynamics are modulated through anti-folding by chaperones · the same entry in another collection · chain A against A, TM-score 1.00
- P0ACG1 · AlphaFold monomer V2.0 prediction for DNA-binding protein stpa (P0ACG1) · a predicted model of the same protein · chain A against A, TM-score 0.42
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 P0ACG1
- Elsewhere: RCSB PDB 2LRX · PDBe 2LRX · UniProt P0ACG1
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