MolNFT v2 · #222415 · protein
Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur cluster assembly pathway
8USQ · DNA repair/transcription protein MET18/MMS19: “Structural and biochemical investigations of a HEAT-repeat protein involved in the cytosolic iron-sulfur…”. Electron microscopy at 12.77, 20 pockets (best druggability 0.83). MolNFT v2…
- PDB
- 8USQ
- Type
- protein
- Length
- 3,928 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 12.77
- Source
- Saccharomyces cerevisiae
- Molecule
- DNA repair/transcription protein MET18/MMS19
- UniProt
- P40469
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · resolution 12.77 · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F, D, C | DNA repair/transcription protein MET18/MMS19 | protein | 982 | 70% helix, 0% strand | P40469 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 858 | 0.83 | 0.85 | 83 | empty |
| 2 | 863 | 0.78 | 0.81 | 87 | empty |
| 3 | 1158 | 0.78 | 0.79 | 91 | empty |
| 4 | 1110 | 0.76 | 0.79 | 99 | empty |
| 5 | 544 | 0.70 | 0.79 | 51 | empty |
Interfaces
4 interfaces between chains.
- A–F · 1964 Ų buried · 15 hydrogen bonds · protein-protein
- D–C · 1586 Ų buried · 13 hydrogen bonds · protein-protein
- F–C · 774 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 349 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- P40469 · AlphaFold monomer V2.0 prediction for DNA REPAIR/TRANSCRIPTION protein MET18/MMS19… · a predicted model of the same protein · chain C against A, TM-score 0.93
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 P40469
- Elsewhere: RCSB PDB 8USQ · PDBe 8USQ · UniProt P40469
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