MolNFT v1 · #129045 · protein
The crystal structure of dfoa bound to FAD, the desferrioxamine biosynthetic pathway cadaverine monooxygenase from the fire blight disease pathogen erwinia amylovora
5O8P · L-lysine 6-monooxygenase involved in desferrioxamine…: “The crystal structure of dfoa bound to FAD, the desferrioxamine biosynthetic pathway cadaverine monooxygenase…”. X-ray diffraction, 1 ligand (FAD), 4 pockets (best druggability…
- PDB
- 5O8P
- Type
- protein
- Length
- 855 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-lysine 6-monooxygenase involved in desferrioxamine biosynthesis
- EC
- 1.14.13.59
- UniProt
- D4I246
- Ligands
- FAD
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-lysine 6-monooxygenase involved in desferrioxamine biosynthesis (EC 1.14.13.59) | protein | 427 | 31% helix, 24% strand | D4I246 |
| B | L-lysine 6-monooxygenase involved in desferrioxamine biosynthesis (EC 1.14.13.59) | protein | 428 | 32% helix, 24% strand | D4I246 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains 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 | 1046 | 0.83 | 0.84 | 92 | empty |
| 2 | 1158 | 0.83 | 0.83 | 112 | FAD |
| 3 | 956 | 0.76 | 0.79 | 72 | empty |
| 4 | 65 | 0.33 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 940 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 5O8P · The crystal structure of DfoA bound to FAD, the desferrioxamine biosynthetic pathway… · the same entry in another collection · chain A against A, TM-score 1.00
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 D4I246
- Elsewhere: RCSB PDB 5O8P · PDBe 5O8P · UniProt D4I246
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