› 5x68

X-ray diffraction
2.1Å resolution

Crystal Structure of Human KMO

Released:
DOI: 10.2210/pdb5x68/pdb
PDB entry 5x68 coloured by chain, front view.
PDB entry 5x68 coloured by chain, side view.
PDB entry 5x68 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Basis for Inhibitor-Induced Hydrogen Peroxide Production by Kynurenine 3-Monooxygenase.
Kim HT, Na BK, Chung J, Kim S, Kwon SK, Cha H, Son J, Cho JM, Hwang KY
Cell Chem Biol 25 426-438.e4 (2018)
PMID: 29429898

Function and Biology Details

Reaction catalysed: 
L-kynurenine + NADPH + O(2) = 3-hydroxy-L-kynurenine + NADP(+) + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127357 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kynurenine 3-monooxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 391 amino acids
Theoretical weight: 44.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: O15229 (Residues: 1-374; Coverage: 77%)
Gene name: KMO
Sequence domains: FAD binding domain
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
1 modified residue:
Ligand MLY 8 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: R3
Unit cell:
a: 176.736Å b: 176.736Å c: 89.434Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.209 0.256
Expression system: Escherichia coli K-12

Quick links

Citations

5 review citations

Advantages of brain penetrating inhibitors of kynurenine-3-monooxygenase for treatment of neurodegenerative diseases.
Zhang et al. (2021)
4 more

6 mentions without citation

Structural and functional characterization of G protein-coupled receptors with deep mutational scanning.
Jones et al. (2020)
5 more