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The crystal structure of dfoa bound to FAD, the desferrioxamine biosynthetic pathway cadaverine monooxygenase from the fire blight disease pathogen erwinia amylovora
Analyse The crystal structure of dfoa bound to FAD, the desferrioxamine biosynthetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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