› 7pyu

X-ray diffraction
1.4Å 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-102689 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
AA9 family lytic polysaccharide monooxygenase A Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 25.26 KDa
Source organism: Panus similis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0S2GKZ1 (Residues: 20-254; Coverage: 100%)
Gene name: LPMO9A
Sequence domains: Auxiliary Activity family 9 (formerly GH61)

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
4 bound ligands:
Ligand CU 1 x CU
Ligand CL 2 x CL
Ligand SO4 4 x SO4
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, DESY BEAMLINE P11
Spacegroup: P41
Unit cell:
a: 48.83Å b: 48.83Å c: 108.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.143 0.142 0.162
Expression system: Escherichia coli

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)