› 4fr0

X-ray diffraction
2.75Å resolution

ArsM arsenic(III) S-adenosylmethionine methyltransferase with SAM

Released:
DOI: 10.2210/pdb4fr0/pdb
PDB entry 4fr0 coloured by chain, front view.
PDB entry 4fr0 coloured by chain, side view.
PDB entry 4fr0 coloured by chain, top view.
Source organism: Cyanidioschyzon sp. 5508
Primary publication:
Structure of an As(III) S-adenosylmethionine methyltransferase: insights into the mechanism of arsenic biotransformation.
Ajees AA, Marapakala K, Packianathan C, Sankaran B, Rosen BP
Biochemistry 51 5476-85 (2012)
PMID: 22712827

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-110992 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methyltransferase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 383 amino acids
Theoretical weight: 42.31 KDa
Source organism: Cyanidioschyzon sp. 5508
Expression system: Escherichia coli
UniProt:
  • Canonical: C0JV69 (Residues: 1-370; Coverage: 93%)
Gene name: arsM
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C222
Unit cell:
a: 67.183Å b: 128.789Å c: 96.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.206 0.283
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Arsenic binding to proteins.
Shen et al. (2013)
15 more

8 mentions without citation

Pathway of human AS3MT arsenic methylation.
Dheeman et al. (2014)
7 more