Research workbench
Flavoprotein 390
Analyse Flavoprotein 390 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FVP
- Type
- protein
- Length
- 462 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavoprotein 390
- UniProt
- P12745
- Ligands
- FMA
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Flavoprotein 390 | protein | 231 | 43% helix, 18% strand | P12745 |
Ligands and binding sites
- FMA · 6-(3-tetradecanoic acid) flavine mononucleotide · ligand · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 750 | 0.82 | 0.85 | 75 | FMA |
| 2 | 426 | 0.73 | 0.83 | 60 | FMA |
| 3 | 137 | 0.66 | 0.87 | 23 | FMA |
| 4 | 171 | 0.65 | 0.84 | 23 | FMA |
| 5 | 236 | 0.52 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1517 Ų buried · 6 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 P12745
- Elsewhere: RCSB PDB 1FVP · PDBe 1FVP · UniProt P12745
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