Research workbench
Crystal structure of mouse tdp-43 RRM2 domain in complex with DNA
Analyse Crystal structure of mouse tdp-43 RRM2 domain in complex with DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D2W
- Type
- protein + DNA
- Length
- 81 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q921F2
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 72 | — | Q921F2 |
| B | — | dna | 9 | — | — |
Compared structures
- 3D2W · Crystal structure of mouse TDP-43 RRM2 domain in complex with DNA · the same entry in another collection · chain A against A, TM-score 1.00
- Q921F2 · AlphaFold monomer V2.0 prediction for tar DNA-binding protein 43 (Q921F2) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q921F2
- Elsewhere: RCSB PDB 3D2W · PDBe 3D2W · UniProt Q921F2
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