4jnd

X-ray diffraction
1.65Å resolution

Structure of a C.elegans sex determining protein

Released:
Source organism: Caenorhabditis elegans
Primary publication:
Structural insight into Caenorhabditis elegans sex-determining protein FEM-2.
J Biol Chem 288 22058-66 (2013)
PMID: 23760267

Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-155964 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein phosphatase fem-2 Chain: A
Molecule details ›
Chain: A
Length: 454 amino acids
Theoretical weight: 51.37 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P49594 (Residues: 1-449; Coverage: 100%)
Gene names: T19C3.8, fem-2
Sequence domains: Protein phosphatase 2C
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 81.399Å b: 160.093Å c: 77.422Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.177 0.202
Expression system: Escherichia coli