5mig

X-ray diffraction
1.35Å resolution

The study of the X-ray induced enzymatic reduction of molecular oxygen to water for laccase from Steccherinum murashkinskyi.The 16-th structure of the series with total exposition time 453 min. The crystal was quick refreezing before this data collection.

Released:

Function and Biology Details

Reaction catalysed:
4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125040 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
laccase Chain: A
Molecule details ›
Chain: A
Length: 546 amino acids
Theoretical weight: 58.58 KDa
Source organism: Steccherinum murashkinskyi
UniProt:
  • Canonical: I1VE66 (Residues: 1-546; Coverage: 100%)
Sequence domains:
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 56.268Å b: 84.415Å c: 112.384Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.141 0.162