› 5mie

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 15-th structure of the series with total exposition time 423 min.

Released:
DOI: 10.2210/pdb5mie/pdb
PDB entry 5mie coloured by chain, front view.
PDB entry 5mie coloured by chain, side view.
PDB entry 5mie coloured by chain, top view.
Source organism: Steccherinum murashkinskyi
Primary publication:
Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water by Steccherinum murashkinskyi laccase: insights into the reaction mechanism.
Polyakov KM, Gavryushov S, Ivanova S, Fedorova TV, Glazunova OA, Popov AN, Koroleva OV
Acta Crystallogr D Struct Biol 73 388-401 (2017)
PMID: 28471364

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
Sequence domains:

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 2 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
Carbohydrate polymer
4 bound ligands:
Ligand CU 4 x CU
Ligand OXY 1 x OXY
Ligand CIT 1 x CIT
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P212121
Unit cell:
a: 56.33Å b: 84.38Å c: 112.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.132 0.148

Quick links

Citations

4 review citations

Laccases: structure, function, and potential application in water bioremediation.
Arregui et al. (2019)
3 more