5h5f

X-ray diffraction
1.7Å resolution

The crystal structure of the yeast arginine methyltransferase SFM1 complexed with SAM

Released:
Primary publication:
A flexible cofactor-binding loop in the novel arginine methyltransferase Sfm1.
FEBS Lett 591 433-441 (2017)
PMID: 27990635

Function and Biology Details

Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-555801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein arginine N-methyltransferase SFM1 Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 27.15 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12314 (Residues: 2-213; Coverage: 100%)
Gene names: OR26.11, SFM1, YOR021C
Sequence domains: Protein arginine N-methyltransferase SFM1-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21
Unit cell:
a: 38.712Å b: 62.417Å c: 44.695Å
α: 90° β: 112.31° γ: 90°
R-values:
R R work R free
0.155 0.154 0.178
Expression system: Escherichia coli