3kci

X-ray diffraction
1.8Å resolution

The third RLD domain of HERC2

Released:
Source organism: Homo sapiens
Entry authors: Walker JR, Qiu L, Vesterberg A, Weigelt J, Bountra C, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S

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 Chain: A
Molecule details ›
Chain: A
Length: 389 amino acids
Theoretical weight: 41.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95714 (Residues: 3951-4321; Coverage: 8%)
Gene name: HERC2
Sequence domains: Regulator of chromosome condensation (RCC1) repeat
Structure domains: Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P61
Unit cell:
a: 52.673Å b: 52.673Å c: 215.242Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.154 0.152 0.195
Expression system: Escherichia coli