Research workbench
AlphaFold monomer V2.0 prediction for naphthalene 1,2-DIOXYGENASE/SALICYLATE 5-hydroxylase systems, ferredoxin-- NAD(P)(+), reductase component (O52378)
Analyse AlphaFold monomer V2.0 prediction for naphthalene 1,2-DIOXYGENASE/SALICYLATE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O52378
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x26ca9158879e824EF8a73775708d1b19082345Fc
- Molecule
- Naphthalene 1,2-DIOXYGENASE/SALICYLATE 5-hydroxylase systems, ferredoxin--NAD(P)(+)…
- UniProt
- O52378
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 22% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Naphthalene 1,2-DIOXYGENASE/SALICYLATE 5-hydroxylase systems, ferredoxin--NAD(P)(+), reductase component | protein | 328 | 22% helix, 33% strand | O52378 |
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 | 502 | 0.70 | 0.80 | 59 | empty |
| 2 | 151 | 0.55 | 0.81 | 20 | empty |
| 3 | 63 | 0.42 | 0.82 | 19 | 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 O52378
- Elsewhere: UniProt O52378 · AlphaFold DB O52378
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