7q40

X-ray diffraction
2.35Å resolution

Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2

Released:
Source organism: Homo sapiens
Entry authors: Demenge A, Howard E, Cousido-Siah A, Mitschler A, Podjarny A, McEwen AG, Trave G

Function and Biology Details

Reaction catalysed:
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-131992 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase HERC2 Chains: A, C, E
Molecule details ›
Chains: A, C, E
Length: 405 amino acids
Theoretical weight: 42.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95714 (Residues: 2938-3342; Coverage: 8%)
Gene name: HERC2
Sequence domains: Regulator of chromosome condensation (RCC1) repeat

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 2
Spacegroup: P43212
Unit cell:
a: 108.54Å b: 108.54Å c: 243.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.23
Expression system: Escherichia coli