Research workbench
A. fumigatus ornithine hydroxylase (sida), reduced state bound to NADP and arg
Analyse A. fumigatus ornithine hydroxylase (sida), reduced state bound to NADP and arg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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