Research workbench
Crystal structure of kynurenine 3-monooxygenase (kmo-394)
Analyse Crystal structure of kynurenine 3-monooxygenase (kmo-394) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J33
- Type
- protein
- Length
- 758 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kynurenine 3-monooxygenase
- EC
- 1.14.13.9
- UniProt
- P38169
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kynurenine 3-monooxygenase (EC 1.14.13.9) | protein | 383 | 35% helix, 28% strand | P38169 |
| B | Kynurenine 3-monooxygenase (EC 1.14.13.9) | protein | 375 | 36% helix, 28% strand | P38169 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 925 | 0.83 | 0.84 | 86 | FAD |
| 2 | 1007 | 0.81 | 0.82 | 87 | FAD |
| 3 | 314 | 0.57 | 0.76 | 50 | empty |
| 4 | 295 | 0.55 | 0.76 | 29 | empty |
| 5 | 55 | 0.26 | 0.72 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 531 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
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 P38169
- Elsewhere: RCSB PDB 4J33 · PDBe 4J33 · UniProt P38169
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