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Electron crystallographic structure of TIA-1 prion-like domain, wild type sequence
Analyse Electron crystallographic structure of TIA-1 prion-like domain, wild type… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VI5
- Type
- protein
- Length
- 10 residues
- Chains
- 1
- Method
- electron crystallography
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.761
- Molecule
- TIA-1 prion-like domain
- UniProt
- P31483
Structure
electron crystallography · resolution 1.761 · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TIA-1 prion-like domain | protein | 10 | 0% helix, 0% strand | P31483 |
Compared structures
- P31483 · AlphaFold monomer V2.0 prediction for nucleolysin tia-1 isoform P40 (P31483) · a predicted model of the same protein · chain A against A, TM-score 0.38
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 P31483
- Elsewhere: RCSB PDB 7VI5 · PDBe 7VI5 · UniProt P31483
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