Research workbench
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase IV subunit 1 (Q9LQ02)
Analyse AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase IV subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9LQ02
- Type
- protein
- Length
- 1,453 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- DNA-directed RNA polymerase IV subunit 1
- UniProt
- Q9LQ02
- Pockets
- 20 · best druggability 0.70
Structure
1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase IV subunit 1 | protein | 1453 | 41% helix, 17% strand | Q9LQ02 |
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 | 972 | 0.70 | 0.74 | 63 | empty |
| 2 | 740 | 0.69 | 0.76 | 49 | empty |
| 3 | 391 | 0.68 | 0.80 | 42 | empty |
| 4 | 505 | 0.66 | 0.77 | 48 | empty |
| 5 | 201 | 0.60 | 0.81 | 37 | empty |
Compared structures
- 8XME · Backtracked Pol IV transcription elongation complex · an experimental structure of the same protein · chain A against A, TM-score 0.75
- 8XMC · Post-translocated Pol IV transcription elongation complex · an experimental structure of the same protein · chain A against A, TM-score 0.75
- 8XMD · Pre-translocated Pol IV transcription elongation complex · an experimental structure of the same protein · chain A against A, TM-score 0.74
- 8XMB · NTP-bound Pol IV transcription elongation complex · an experimental structure of the same protein · chain A against A, TM-score 0.74
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 Q9LQ02
- Elsewhere: UniProt Q9LQ02 · AlphaFold DB Q9LQ02
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