MolNFT v1 · #5535 · protein + RNA
NMR structure of the complex between the third dsrbd from drosophila staufen and a RNA hairpin
1EKZ · Staufen double-stranded RNA binding domain: “NMR structure of the complex between the third dsrbd from drosophila staufen and a RNA hairpin”. Solution nmr, 2 pockets (best druggability 0.35). MolNFT v1 #5535 on GenesisL1: 3D…
- PDB
- 1EKZ
- Type
- protein + RNA
- Length
- 106 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Staufen double-stranded RNA binding domain; Maternal effect protein (staufen)
- UniProt
- P25159
- Pockets
- 2 · best druggability 0.35
Structure
solution nmr · 2 distinct chains · 29% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Staufen double-stranded RNA binding domain | rna | 30 | — | — |
| A | Maternal effect protein (staufen) | protein | 76 | 29% helix, 18% strand | P25159 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.35 | 0.72 | 14 | empty |
| 2 | 88 | 0.33 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- B–A · 526 Ų buried · 13 hydrogen bonds · protein-nucleic
Compared structures
- 1EKZ · NMR structure of the complex between the third dsrbd from drosophila staufen and a RNA… · the same entry in another collection · chain B against B, TM-score 1.00
- P25159 · AlphaFold monomer V2.0 prediction for maternal effect protein staufen (P25159) · a predicted model of the same protein · chain A against A, TM-score 0.73
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 P25159
- Elsewhere: RCSB PDB 1EKZ · PDBe 1EKZ · UniProt P25159
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