› 7d4d

X-ray diffraction
2.29Å resolution

Structure of L-lysine oxidase precursor in complex with L-lysine (1.24M)

Released:
DOI: 10.2210/pdb7d4d/pdb
PDB entry 7d4d coloured by chain, front view.
PDB entry 7d4d coloured by chain, side view.
PDB entry 7d4d coloured by chain, top view.
Source organism: Trichoderma viride
Primary publication:
Structural basis of enzyme activity regulation by the propeptide of l-lysine α-oxidase precursor from Trichoderma viride.
Kitagawa M, Ito N, Matsumoto Y, Saito M, Tamura T, Kusakabe H, Inagaki K, Imada K
OpenAccess logo J Struct Biol X 5 100044 (2021)
PMID: 33554108

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101363 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amine oxidase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 617 amino acids
Theoretical weight: 69.57 KDa
Source organism: Trichoderma viride
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0G4DCU0 (Residues: 1-617; Coverage: 100%)
Gene name: LysOX
Sequence domains: Flavin containing amine oxidoreductase

Ligands and Environments

2 bound ligands:
Ligand FAD 1 x FAD
Ligand LYS 1 x LYS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2221
Unit cell:
a: 94.31Å b: 127.96Å c: 94.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.221
Expression system: Escherichia coli

Quick links

Citations

1 review citation

L-Lysine α-Oxidase: Enzyme with Anticancer Properties.
Lukasheva et al. (2021)
1 other article

1 mention without citation

Structural basis of enzyme activity regulation by the propeptide of l-lysine α-oxidase precursor from Trichoderma viride.
Kitagawa et al. (2021)