Research workbench
Solution structure of G-quadruplex recognition domain of rhau
Analyse Solution structure of G-quadruplex recognition domain of rhau in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N16
- Type
- protein
- Length
- 20 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent RNA helicase DHX36
- EC
- 3.6.4.12, 3.6.4.13
- UniProt
- Q9H2U1
Structure
solution nmr · 1 distinct chain · 30% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase DHX36 (EC 3.6.4.12, 3.6.4.13) | protein | 20 | 30% helix, 0% strand | Q9H2U1 |
Compared structures
- 2N16 · Solution structure of G-quadruplex recognition domain of RHAU · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H2U1 · AlphaFold monomer V2.0 prediction for ATP-dependent DNA/RNA helicase DHX36 (Q9H2U1) · a predicted model of the same protein · chain A against A, TM-score 0.25
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 Q9H2U1
- Elsewhere: RCSB PDB 2N16 · PDBe 2N16 · UniProt Q9H2U1
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