MolNFT v1 · #95861 · protein
Crystal structure of kynurenine 3-monooxygenase (kmo-396PROT)
4J31: “Crystal structure of kynurenine 3-monooxygenase (kmo-396PROT)”. X-ray diffraction, 1 ligand (FAD), 6 pockets (best druggability 0.81). MolNFT v1 #95861 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4J31
- Type
- protein
- Length
- 741 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
- 6 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kynurenine 3-monooxygenase (EC 1.14.13.9) | protein | 366 | 35% helix, 30% strand | P38169 |
| B | Kynurenine 3-monooxygenase (EC 1.14.13.9) | protein | 375 | 34% helix, 30% 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
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 892 | 0.81 | 0.83 | 73 | FAD |
| 2 | 893 | 0.81 | 0.83 | 76 | FAD |
| 3 | 366 | 0.58 | 0.76 | 33 | empty |
| 4 | 98 | 0.43 | 0.79 | 25 | empty |
| 5 | 100 | 0.39 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 536 Ų buried · 12 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 4J31 · PDBe 4J31 · UniProt P38169
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.