› 2a2p

Solution NMR

Solution structure of SelM from Mus musculus

Released:
DOI: 10.2210/pdb2a2p/pdb
PDB entry 2a2p coloured by chain, ensemble of 20 models, front view.
PDB entry 2a2p coloured by chain, ensemble of 20 models, side view.
PDB entry 2a2p coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family.
Ferguson AD, Labunskyy VM, Fomenko DE, Araç D, Chelliah Y, Amezcua CA, Rizo J, Gladyshev VN, Deisenhofer J
J Biol Chem 281 3536-43 (2006)
PMID: 16319061

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186582 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Selenoprotein M Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 15.06 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8VHC3 (Residues: 25-145; Coverage: 99%)
Gene name: Selenom
Sequence domains: Sep15/SelM redox domain
Structure domains: Sep15/SelM thioredoxin-like domain, active-site redox motif

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: Distance geometry Simulated annealing Molecular dynamics Torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

44 review citations

From selenium to selenoproteins: synthesis, identity, and their role in human health.
Papp et al. (2007)
43 more

1 mention without citation

Selenocysteine-Mediated Expressed Protein Ligation of SELENOM.
Liu et al. (2018)