› 7ze9

X-ray diffraction
2.65Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-214649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Chitin-binding type-4 domain-containing protein Chains: AAA, BBB, CCC
Molecule details ›
Chains: AAA, BBB, CCC
Length: 188 amino acids
Theoretical weight: 20.51 KDa
Source organism: Thermothelomyces thermophilus
Expression system: Thermothelomyces thermophilus
UniProt:
  • Canonical: G2QH80 (Residues: 1-188; Coverage: 100%)
Gene name: MYCTH_2306267
Sequence domains: Lytic polysaccharide mono-oxygenase, cellulose-degrading

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
3 bound ligands:
Ligand NAG 3 x NAG
Ligand CU 3 x CU
Ligand ACT 1 x ACT
1 modified residue:
Ligand HIC 3 x HIC

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-3
Spacegroup: C2
Unit cell:
a: 152.424Å b: 52.154Å c: 88.855Å
α: 90° β: 105.666° γ: 90°
R-values:
R R work R free
0.18 0.178 0.233
Expression system: Thermothelomyces thermophilus

Quick links

Citations

1 review citation

Expanding the catalytic landscape of metalloenzymes with lytic polysaccharide monooxygenases.
Munzone et al. (2024)
2 other articles

1 mention without citation

AA16 Oxidoreductases Boost Cellulose-Active AA9 Lytic Polysaccharide Monooxygenases from Myceliophthora thermophila.
Sun et al. (2023)