› 7pz5

X-ray diffraction
1.45Å resolution

Function and Biology Details

Reaction catalysed: 
((1->4)-beta-D-glucosyl)(n+m) + reduced acceptor + O(2) = 4-dehydro-beta-D-glucosyl-((1->4)-beta-D-glucosyl)(n-1) + ((1->4)-beta-D-glucosyl)(m) + acceptor + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AA9 family lytic polysaccharide monooxygenase A Chain: A
Molecule details ›
Chain: A
Length: 228 amino acids
Theoretical weight: 24.42 KDa
Source organism: Thermoascus aurantiacus
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: G3XAP7 (Residues: 1-228; Coverage: 100%)
Gene name: LPMO9A
Sequence domains: Auxiliary Activity family 9 (formerly GH61)

Ligands and Environments

4 bound ligands:
Ligand CU 1 x CU
Ligand AKR 1 x AKR
Ligand NAG 1 x NAG
Ligand EPE 1 x EPE
1 modified residue:
Ligand HIC 1 x HIC

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: P21
Unit cell:
a: 34.41Å b: 87.29Å c: 37.41Å
α: 90° β: 104.91° γ: 90°
R-values:
R R work R free
0.167 0.166 0.186
Expression system: Aspergillus oryzae

Quick links

Citations

1 review citation

Molecular Mechanism of Substrate Oxidation in Lytic Polysaccharide Monooxygenases: Insight from Theoretical Investigations.
Hagemann et al. (2023)
5 other articles

1 mention without citation

Changes in active-site geometry on X-ray photoreduction of a lytic polysaccharide monooxygenase active-site copper and saccharide binding.
Tandrup et al. (2022)