Research workbench
Structure of S. cerevisiae DOM34, a translation termination-like factor involved in RNA quality control pathways and interacting with HBS1 (unlabeled protein)
Analyse Structure of S. cerevisiae DOM34, a translation termination-like factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VGM
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DOM34
- UniProt
- P33309
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DOM34 | protein | 354 | 34% helix, 27% strand | P33309 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 885 | 0.76 | 0.79 | 48 | empty |
| 2 | 72 | 0.41 | 0.79 | 20 | empty |
Compared structures
- 2VGM · Structure of S. cerevisiae Dom34, a translation termination-like factor involved in RNA… · the same entry in another collection · chain A against A, TM-score 1.00
- P33309 · AlphaFold monomer V2.0 prediction for protein DOM34 (P33309) · a predicted model of the same protein · chain A against A, TM-score 0.71
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
- Elsewhere: RCSB PDB 2VGM · PDBe 2VGM · UniProt P33309
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