MolNFT v1 · #265869 · protein
AlphaFold monomer V2.0 prediction for nf-kappa-B-repressing factor (O15226)
O15226: “AlphaFold monomer V2.0 prediction for nf-kappa-B-repressing factor (O15226)”. 8 pockets (best druggability 0.53). MolNFT v1 #265869 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- O15226
- Type
- protein
- Length
- 690 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x064FA49c6b8dFe284029F65208DDf88b7F02240e
- Molecule
- Nf-kappa-B-repressing factor
- UniProt
- O15226
- Pockets
- 8 · best druggability 0.53
Structure
1 distinct chain · 28% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nf-kappa-B-repressing factor | protein | 690 | 28% helix, 17% strand | O15226 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.53 | 0.76 | 26 | empty |
| 2 | 106 | 0.50 | 0.81 | 20 | empty |
| 3 | 174 | 0.46 | 0.75 | 22 | empty |
| 4 | 132 | 0.43 | 0.76 | 19 | empty |
| 5 | 121 | 0.42 | 0.76 | 21 | empty |
Compared structures
- 6SH7 · Crystal structure of the human deah-helicase DHX15 in complex with the nkrf G-patch · an experimental structure of the same protein · chain A against B, TM-score 0.05
- 6SH7 · Crystal structure of the human DEAH-helicase DHX15 in complex with the NKRF G-patch · an experimental structure of the same protein · chain A against B, TM-score 0.05
- 6SH6 · Crystal structure of the human deah-helicase DHX15 in complex with the nkrf G-patch bound… · an experimental structure of the same protein · chain A against B, TM-score 0.04
- 6SH6 · Crystal structure of the human DEAH-helicase DHX15 in complex with the NKRF G-patch bound… · an experimental structure of the same protein · chain A against B, TM-score 0.04
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 O15226
- Elsewhere: UniProt O15226 · AlphaFold DB O15226
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