› 7jya

X-ray diffraction
2.46Å resolution

Crystal structure of E3 ligase in complex with peptide

Released:
DOI: 10.2210/pdb7jya/pdb
PDB entry 7jya coloured by chain, front view.
PDB entry 7jya coloured by chain, side view.
PDB entry 7jya coloured by chain, top view.
Source organisms:
Primary publication:
Molecular basis for ubiquitin ligase CRL2FEM1C-mediated recognition of C-degron.
Yan X, Wang X, Li Y, Zhou M, Li Y, Song L, Mi W, Min J, Dong C
Nat Chem Biol 17 263-271 (2021)
PMID: 33398170

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188586 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein fem-1 homolog C Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 371 amino acids
Theoretical weight: 41.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96JP0 (Residues: 2-371; Coverage: 60%)
Gene names: FEM1C, KIAA1785
Sequence domains: Ankyrin repeats (3 copies)
Protein Rev Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 11 amino acids
Theoretical weight: 1.68 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Not provided
UniProt:
  • Canonical: P04618 (Residues: 40-50; Coverage: 10%)
Gene name: rev

Ligands and Environments

1 bound ligand:
Ligand UNX 5 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P41212
Unit cell:
a: 100.133Å b: 100.133Å c: 287.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.26
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

2 review citations

How the ends signal the end: Regulation by E3 ubiquitin ligases recognizing protein termini.
Sherpa et al. (2022)
1 more