› 3g5f

X-ray diffraction
1.4Å resolution

Function and Biology Details

Reaction catalysed: 
Cyclo(L-tyrosyl-L-tyrosyl) + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = mycocyclosin + 2 oxidized ferredoxin [iron-sulfur] cluster + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-162003 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mycocyclosin synthase Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 43.31 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WPP7 (Residues: 1-396; Coverage: 100%)
Gene names: MTCY339.34c, Rv2276, cyp121
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand HEM 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6522
Unit cell:
a: 77.373Å b: 77.373Å c: 264.05Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.159 0.19
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Oxidative Cyclization in Natural Product Biosynthesis.
Tang et al. (2017)
23 more

8 mentions without citation

Conformational plasticity and structure/function relationships in cytochromes P450.
Pochapsky et al. (2010)
7 more