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Crystal Structure of kynurenine 3-monooxygenase (KMO-396Prot)
Analyse Crystal Structure of kynurenine 3-monooxygenase (KMO-396Prot) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J31
- Type
- protein
- Length
- 741 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.4
- Source
- Saccharomyces cerevisiae
- Molecule
- Kynurenine 3-monooxygenase
- EC
- 1.14.13.9
- UniProt
- P38169
- Ligands
- FAD
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.4 · 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
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