2bry

X-ray diffraction
1.45Å resolution

Crystal structure of the native monooxygenase domain of MICAL at 1.45 A resolution

Released:
Model geometry
Fit model/data
Data not analysed

Function and Biology Details

Reactions catalysed:
[F-actin]-L-methionine + NADPH + O(2) + H(+) = [F-actin]-L-methionine-(R)-S-oxide + NADP(+) + H(2)O
NAD(P)H + O(2) = NAD(P)(+) + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-186566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
[F-actin]-monooxygenase MICAL1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 497 amino acids
Theoretical weight: 55.24 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8VDP3 (Residues: 1-489; Coverage: 47%)
Gene names: Mical, Mical1, Nical
Sequence domains: FAD binding domain
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
3 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 76.588Å b: 89.548Å c: 83.458Å
α: 90° β: 114.35° γ: 90°
R-values:
R R work R free
0.181 0.18 0.222
Expression system: Escherichia coli