Research workbench
AlphaFold monomer V2.0 prediction for polyribonucleotide nucleotidyltransferase (B9MEL0)
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
- B9MEL0
- Type
- protein
- Length
- 727 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd92eb9B6Bd45d2c5FBB3651b469A6CA52af64a1D
- Molecule
- Polyribonucleotide nucleotidyltransferase
- UniProt
- B9MEL0
- Pockets
- 4 · best druggability 0.76
Structure
1 distinct chain · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyribonucleotide nucleotidyltransferase | protein | 727 | 33% helix, 28% strand | B9MEL0 |
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 | 953 | 0.76 | 0.79 | 88 | empty |
| 2 | 1034 | 0.71 | 0.75 | 87 | empty |
| 3 | 65 | 0.43 | 0.81 | 14 | empty |
| 4 | 66 | 0.33 | 0.76 | 16 | 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 B9MEL0
- Elsewhere: UniProt B9MEL0 · AlphaFold DB B9MEL0
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