› 2ogb

X-ray diffraction
1.95Å resolution

Crystal structure of the C-terminal domain of mouse Nrdp1

Released:
DOI: 10.2210/pdb2ogb/pdb
PDB entry 2ogb coloured by chain, front view.
PDB entry 2ogb coloured by chain, side view.
PDB entry 2ogb coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3.
Bouyain S, Leahy DJ
Protein Sci 16 654-61 (2007)
PMID: 17384230

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-183869 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase NRDP1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 14.51 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8BH75 (Residues: 193-317; Coverage: 39%)
Gene names: Flrf, Nrdp1, Rnf41
Sequence domains: USP8 interacting

Ligands and Environments

2 bound ligands:
Ligand SCN 1 x SCN
Ligand GOL 2 x GOL
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2
Unit cell:
a: 157.427Å b: 58.227Å c: 37.387Å
α: 90° β: 101.53° γ: 90°
R-values:
R R work R free
0.213 0.212 0.234
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Targeting ubiquitination for cancer therapies.
Morrow et al. (2015)
2 more

1 mention without citation

Structure-based mutagenesis of the substrate-recognition domain of Nrdp1/FLRF identifies the binding site for the receptor tyrosine kinase ErbB3.
Bouyain et al. (2007)