Research workbench
Crystal structure of the EIF2 alpha subunit from saccharomyces cerevisia
Analyse Crystal structure of the EIF2 alpha subunit from saccharomyces cerevisia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q46
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translation initiation factor 2 alpha subunit
- UniProt
- P20459
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translation initiation factor 2 alpha subunit | protein | 174 | 43% helix, 21% strand | P20459 |
Compared structures
- 1Q46 · crystal structure of the eIF2 alpha subunit from saccharomyces cerevisia · the same entry in another collection · chain A against A, TM-score 1.00
- P20459 · AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 2 subunit… · 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 P20459
- Elsewhere: RCSB PDB 1Q46 · PDBe 1Q46 · UniProt P20459
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