Research workbench
Crystal structure of the first dsrbd of tar RNA-binding protein 2
Analyse Crystal structure of the first dsrbd of tar RNA-binding protein 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LLH
- Type
- protein
- Length
- 130 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Risc-loading complex subunit TARBP2
- UniProt
- Q15633
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Risc-loading complex subunit TARBP2 | protein | 64 | 42% helix, 33% strand | Q15633 |
| B | Risc-loading complex subunit TARBP2 | protein | 66 | 41% helix, 35% strand | Q15633 |
Ligands and binding sites
- MLI · Malonate ion · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 444 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3LLH · Crystal structure of the first dsRBD of TAR RNA-binding protein 2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q15633 · AlphaFold monomer V2.0 prediction for risc-loading complex subunit TARBP2 (Q15633) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q15633
- Elsewhere: RCSB PDB 3LLH · PDBe 3LLH · UniProt Q15633
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