7el6

X-ray diffraction
2.8Å resolution

Structure of SMCR8 bound FEM1B

Released:
Source organism: Homo sapiens
Primary publication:
Structural insights into SMCR8 C-degron recognition by FEM1B.
Biochem Biophys Res Commun 557 236-239 (2021)
PMID: 33892462

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-186256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanine nucleotide exchange protein SMCR8; Protein fem-1 homolog B Chains: A, B
Molecule details ›
Chains: A, B
Length: 357 amino acids
Theoretical weight: 39.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UK73 (Residues: 1-337; Coverage: 54%)
  • Canonical: Q8TEV9 (Residues: 778-787; Coverage: 1%)
Gene names: F1AA, FEM1B, KIAA0396, SMCR8
Sequence domains: Ankyrin repeats (3 copies)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21212
Unit cell:
a: 83.306Å b: 91.497Å c: 112.148Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.203 0.266
Expression system: Escherichia coli