› 6ve0

X-ray diffraction
3.15Å resolution

Crystal structure of reduced SfmD by soaking with sodium hydrosulfite

Released:
DOI: 10.2210/pdb6ve0/pdb
PDB entry 6ve0 coloured by chain, front view.
PDB entry 6ve0 coloured by chain, side view.
PDB entry 6ve0 coloured by chain, top view.
Source organism: Streptomyces lavendulae
Primary publication:
A novel catalytic heme cofactor in SfmD with a single thioether bond and a bis-His ligand set revealed by a de novo crystal structural and spectroscopic study.
Shin I, Davis I, Nieves-Merced K, Wang Y, McHardy S, Liu A
Chem Sci 12 3984-3998 (2021)
PMID: 34163669

Function and Biology Details

Reaction catalysed: 
3-methyl-L-tyrosine + H(2)O(2) = 3-hydroxy-5-methyl-L-tyrosine + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109131 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-methyl-L-tyrosine peroxygenase Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 38.23 KDa
Source organism: Streptomyces lavendulae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B0CN28 (Residues: 1-365; Coverage: 100%)
Gene name: sfmD

Ligands and Environments


Cofactor: Ligand HEC 1 x HEC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P3121
Unit cell:
a: 59.453Å b: 59.453Å c: 159.965Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.265 0.26 0.308
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Molecular Rationale for Partitioning between C-H and C-F Bond Activation in Heme-Dependent Tyrosine Hydroxylase.
Wang et al. (2021)
2 more

1 mention without citation

A novel catalytic heme cofactor in SfmD with a single thioether bond and a bis-His ligand set revealed by a de novo crystal structural and spectroscopic study.
Shin et al. (2021)