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X-ray diffraction
2.2Å resolution

L-amino acid oxidase 4 (HcLAAO4) from the fungus Hebeloma cylindrosporum in complex with L-phenylalanine

Released:
DOI: 10.2210/pdb9enk/pdb
PDB entry 9enk coloured by chain, front view.
PDB entry 9enk coloured by chain, side view.
PDB entry 9enk coloured by chain, top view.
Source organism: Hebeloma cylindrosporum
Primary publication:
Crystal structure and enzyme engineering of the broad substrate spectrum l-amino acid oxidase 4 from the fungus Hebeloma cylindrosporum.
Koopmeiners S, Gilzer D, Widmann C, Berelsmann N, Sproß J, Niemann HH, Fischer von Mollard G
FEBS Lett (2024)
PMID: 39152524

Function and Biology Details

Reaction catalysed: 
An L-amino acid + H(2)O + O(2) = a 2-oxo carboxylate + NH(3) + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-278865 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-amino acid oxidase 4 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 562 amino acids
Theoretical weight: 62.2 KDa
Source organism: Hebeloma cylindrosporum
Expression system: Escherichia coli
UniProt:
  • Canonical: S4S6Z0 (Residues: 54-615; Coverage: 92%)
Sequence domains: Flavin containing amine oxidoreductase

Ligands and Environments


Cofactor: Ligand FDA 4 x FDA
3 bound ligands:
Ligand PHE 4 x PHE
Ligand SO4 41 x SO4
Ligand PGR 9 x PGR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-3
Spacegroup: P21
Unit cell:
a: 84.7Å b: 131.73Å c: 107.46Å
α: 90° β: 96.04° γ: 90°
R-values:
R R work R free
0.172 0.17 0.202
Expression system: Escherichia coli

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