› 5t38

X-ray diffraction
1.15Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-103300 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methyltransferase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 254 amino acids
Theoretical weight: 28.33 KDa
Source organism: Micromonospora carbonacea
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A1C5AE13 (Residues: 1-233; Coverage: 52%)
Gene name: GA0070563_112238
Sequence domains: Methyltransferase domain

Ligands and Environments

1 bound ligand:
Ligand SAH 1 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 51.427Å b: 41.272Å c: 56.465Å
α: 90° β: 99.8° γ: 90°
R-values:
R R work R free
0.154 0.153 0.168
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases.
Rajakovich et al. (2019)
1 more

1 mention without citation

The Structure of the Bifunctional Everninomicin Biosynthetic Enzyme EvdMO1 Suggests Independent Activity of the Fused Methyltransferase-Oxidase Domains.
Starbird et al. (2018)