› 4e15

X-ray diffraction
1.5Å resolution

Crystal structure of kynurenine formamidase conjugated with an inhibitor

Released:
DOI: 10.2210/pdb4e15/pdb
PDB entry 4e15 coloured by chain, front view.
PDB entry 4e15 coloured by chain, side view.
PDB entry 4e15 coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster.
Han Q, Robinson H, Li J
Biochem J 446 253-60 (2012)
PMID: 22690733

Function and Biology Details

Reaction catalysed: 
N-formyl-L-kynurenine + H(2)O = formate + L-kynurenine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194279 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kynurenine formamidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 35.37 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9VMC9 (Residues: 1-300; Coverage: 100%)
Gene names: CG9542, KFase
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand EDO 5 x EDO
1 modified residue:
Ligand SEB 2 x SEB

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2221
Unit cell:
a: 71.602Å b: 76.021Å c: 210.377Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.171 0.198
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Role of Nicotinamide Adenine Dinucleotide and Related Precursors as Therapeutic Targets for Age-Related Degenerative Diseases: Rationale, Biochemistry, Pharmacokinetics, and Outcomes.
Braidy et al. (2019)
1 more

2 mentions without citation

Global methylation profiling of lung cancer identifies novel methylated genes.
Dai et al. (2001)
1 more