Research workbench
A. fumigatus ornithine hydroxylase (sida) bound to NADP and lysine
Analyse A. fumigatus ornithine hydroxylase (sida) bound to NADP and lysine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B64
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-ornithine N5 monooxygenase
- UniProt
- Q5SE95
- Ligands
- LYS, FAD, NAP, SO4
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-ornithine N5 monooxygenase | protein | 454 | 34% helix, 21% strand | Q5SE95 |
Ligands and binding sites
- LYS · Lysine · ligand · chains A
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 8 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 | 954 | 0.83 | 0.84 | 73 | LYS, FAD, NAP |
| 2 | 142 | 0.47 | 0.77 | 29 | empty |
| 3 | 94 | 0.45 | 0.79 | 16 | empty |
| 4 | 81 | 0.40 | 0.78 | 15 | empty |
| 5 | 92 | 0.36 | 0.74 | 16 | GOL |
Compared structures
- 4B64 · A. fumigatus ornithine hydroxylase (SidA) bound to NADP and Lysine · 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 4B64 · PDBe 4B64 · UniProt Q5SE95
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