Research workbench
Structure of the DOM34-HBS1-gdpnp complex bound to a translating ribosome
Analyse Structure of the DOM34-HBS1-gdpnp complex bound to a translating ribosome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IZQ
- Type
- protein
- Length
- 902 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein DOM34; Elongation factor 1 alpha-like protein
- EC
- 3.1.-.-
- UniProt
- P33309, P32769
- Pockets
- 13 · best druggability 0.84
Structure
electron microscopy · 2 distinct chains · 25% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 0 | Protein DOM34 (EC 3.1.-.-) | protein | 386 | 28% helix, 23% strand | P33309 |
| 1 | Elongation factor 1 alpha-like protein | protein | 516 | 22% helix, 24% strand | P32769 |
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1055 | 0.84 | 0.85 | 110 | empty |
| 2 | 393 | 0.73 | 0.84 | 41 | empty |
| 3 | 57 | 0.71 | 0.97 | 30 | empty |
| 4 | 487 | 0.70 | 0.80 | 59 | empty |
| 5 | 63 | 0.67 | 0.94 | 19 | empty |
Interfaces
1 interface between chains.
- 0–1 · 1655 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 3IZQ · Structure of the Dom34-Hbs1-GDPNP complex bound to a translating ribosome · the same entry in another collection · chain 0 against 0, TM-score 1.00
- P33309 · AlphaFold monomer V2.0 prediction for protein DOM34 (P33309) · a predicted model of the same protein · chain 0 against A, TM-score 0.73
- P32769 · AlphaFold monomer V2.0 prediction for elongation factor 1 alpha-like protein (P32769) · a predicted model of the same protein · chain 1 against A, TM-score 0.72
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 P33309
- Every structure of UniProt P32769
- Elsewhere: RCSB PDB 3IZQ · PDBe 3IZQ · UniProt P33309 · UniProt P32769
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