› 2ing

X-ray diffraction
3.6Å resolution

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-153627 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Breast cancer type 1 susceptibility protein Chain: X
Molecule details ›
Chain: X
Length: 213 amino acids
Theoretical weight: 24.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P38398 (Residues: 1649-1859; Coverage: 11%)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain

Ligands and Environments

2 bound ligands:
Ligand CO 1 x CO
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P6122
Unit cell:
a: 114.34Å b: 114.34Å c: 119.878Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.251 0.247 0.302
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

On the role of electrostatics in protein-protein interactions.
Zhang et al. (2011)
4 more

7 mentions without citation

Fanconi anemia pathway as a prospective target for cancer intervention.
Liu et al. (2020)
6 more