Research workbench
Structure of reduced sida ornithine hydroxylase with the FAD "in" and complexed with NADP and L-ornithine
Analyse Structure of reduced sida ornithine hydroxylase with the FAD "in" and complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X0J
- Type
- protein
- Length
- 1,811 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E9QYP0
- Ligands
- NAP, FDA
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 452 | — | E9QYP0 |
| B | — | protein | 456 | — | E9QYP0 |
| C | — | protein | 452 | — | E9QYP0 |
| D | — | protein | 451 | — | E9QYP0 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- FDA · Dihydroflavine-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6X0J · Structure of reduced SidA ornithine hydroxylase with the FAD in" and complexed with NADP… · the same entry in another collection · chain B against B, TM-score 1.00
- E9QYP0 · AlphaFold monomer V2.0 prediction for L-ornithine N(5)-monooxygenase (E9QYP0) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 E9QYP0
- Elsewhere: RCSB PDB 6X0J · PDBe 6X0J · UniProt E9QYP0
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