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AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (B0C1M5)
Analyse AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B0C1M5
- Type
- protein
- Length
- 716 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x04726090273ee3Cf442C951969BB1de9607d29f6
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- B0C1M5
- Pockets
- 6 · best druggability 0.74
Structure
1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 716 | 36% helix, 29% strand | B0C1M5 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 503 | 0.74 | 0.82 | 44 | empty |
| 2 | 658 | 0.67 | 0.76 | 62 | empty |
| 3 | 226 | 0.56 | 0.78 | 36 | empty |
| 4 | 154 | 0.40 | 0.73 | 20 | empty |
| 5 | 81 | 0.33 | 0.74 | 15 | 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 B0C1M5
- Elsewhere: UniProt B0C1M5 · AlphaFold DB B0C1M5
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