MolNFT v1 · #86423 · protein
A. fumigatus ornithine hydroxylase (sida), reduced state bound to NADP and arg
4B66 · L-ornithine N5 monooxygenase: “A. fumigatus ornithine hydroxylase (sida), reduced state bound to NADP and arg”. X-ray diffraction, 4 ligands (ARG, FAD, NAP), 5 pockets (best druggability 0.81). MolNFT v1 #86423 on GenesisL1: 3D…
- PDB
- 4B66
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-ornithine N5 monooxygenase
- UniProt
- Q5SE95
- Ligands
- ARG, FAD, NAP, SO4
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-ornithine N5 monooxygenase | protein | 448 | 33% helix, 22% strand | Q5SE95 |
Ligands and binding sites
- ARG · Arginine · ligand · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1131 | 0.81 | 0.82 | 92 | ARG, FAD, NAP, GOL |
| 2 | 84 | 0.40 | 0.78 | 16 | empty |
| 3 | 104 | 0.40 | 0.75 | 16 | GOL |
| 4 | 57 | 0.31 | 0.76 | 12 | empty |
| 5 | 61 | 0.29 | 0.74 | 12 | empty |
Compared structures
- 4B66 · A. fumigatus ornithine hydroxylase (SidA), reduced state bound to NADP and Arg · 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 Q5SE95
- Elsewhere: RCSB PDB 4B66 · PDBe 4B66 · UniProt Q5SE95
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