MolNFT v1 · #280601 · protein
AlphaFold monomer V2.0 prediction for prolyl 3,4-dihydroxylase OFD1 (Q11120)
Q11120: “AlphaFold monomer V2.0 prediction for prolyl 3,4-dihydroxylase OFD1 (Q11120)”. 3 pockets (best druggability 0.74). MolNFT v1 #280601 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q11120
- Type
- protein
- Length
- 515 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- Prolyl 3,4-dihydroxylase OFD1
- UniProt
- Q11120
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl 3,4-dihydroxylase OFD1 | protein | 515 | 28% helix, 27% strand | Q11120 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 993 | 0.74 | 0.77 | 93 | empty |
| 2 | 93 | 0.52 | 0.83 | 20 | empty |
| 3 | 71 | 0.35 | 0.76 | 18 | empty |
Compared structures
- 6E0T · C-terminal domain of fission yeast OFD1 · an experimental structure of the same protein · chain A against X, TM-score 0.47
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 Q11120
- Elsewhere: UniProt Q11120 · AlphaFold DB Q11120
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