MolNFT v1 · #181210 · protein
FAD-dependent monooxygenase afod from a. nidulans
7LO1: “FAD-dependent monooxygenase afod from a. nidulans”. X-ray diffraction, 2 ligands (FAD, SO4), 4 pockets (best druggability 0.84). MolNFT v1 #181210 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7LO1
- Type
- protein
- Length
- 844 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAD-dependent monooxygenase afod
- EC
- 1.-.-.-
- UniProt
- Q5BEJ7
- Ligands
- FAD, SO4
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | FAD-dependent monooxygenase afod (EC 1.-.-.-) | protein | 422 | 41% helix, 25% strand | Q5BEJ7 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1087 | 0.84 | 0.85 | 100 | FAD |
| 2 | 1085 | 0.81 | 0.82 | 89 | FAD |
| 3 | 277 | 0.50 | 0.74 | 37 | empty |
| 4 | 69 | 0.40 | 0.80 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 325 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 Q5BEJ7
- Elsewhere: RCSB PDB 7LO1 · PDBe 7LO1 · UniProt Q5BEJ7
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