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Crystal structure of A/EIF2ALPHA-ADIM2P-rRNA complex from pyrococcus horikoshii OT3
Analyse Crystal structure of A/EIF2ALPHA-ADIM2P-rRNA complex from pyrococcus horikoshii… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AEV
- Type
- protein + RNA
- Length
- 356 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Translation initiation factor 2 subunit alpha; Putative uncharacterized protein PH1566…
- UniProt
- O58655, O59282
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 52% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translation initiation factor 2 subunit alpha | protein | 168 | 47% helix, 23% strand | O58655 |
| B | Putative uncharacterized protein PH1566 | protein | 177 | 56% helix, 18% strand | O59282 |
| C | RNA (5'-R(*GP*GP*AP*UP*CP*AP*CP*CP*UP*CP*C)-3') | rna | 11 | — | — |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 252 | 0.56 | 0.77 | 38 | empty |
| 2 | 259 | 0.52 | 0.75 | 38 | empty |
Interfaces
2 interfaces between chains.
- B–C · 1216 Ų buried · 28 hydrogen bonds · protein-nucleic
- A–B · 955 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3AEV · Crystal structure of a/eIF2alpha-aDim2p-rRNA complex from Pyrococcus horikoshii OT3 · the same entry in another collection · chain A against A, TM-score 1.00
- O58655 · AlphaFold monomer V2.0 prediction for translation initiation factor 2 subunit alpha… · 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 O58655
- Every structure of UniProt O59282
- Elsewhere: RCSB PDB 3AEV · PDBe 3AEV · UniProt O58655 · UniProt O59282
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