Research workbench
AlphaFold monomer V2.0 prediction for ribosomal protein S12 methylthiotransferase rimo (Q4KHA5)
Analyse AlphaFold monomer V2.0 prediction for ribosomal protein S12… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4KHA5
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- Ribosomal protein S12 methylthiotransferase rimo
- UniProt
- Q4KHA5
- Pockets
- 4 · best druggability 0.75
Structure
1 distinct chain · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosomal protein S12 methylthiotransferase rimo | protein | 445 | 34% helix, 23% strand | Q4KHA5 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 538 | 0.75 | 0.83 | 52 | empty |
| 2 | 214 | 0.50 | 0.76 | 24 | empty |
| 3 | 63 | 0.36 | 0.78 | 16 | empty |
| 4 | 62 | 0.27 | 0.73 | 18 | empty |
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 Q4KHA5
- Elsewhere: UniProt Q4KHA5 · AlphaFold DB Q4KHA5
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