PDBe 4o2w

X-ray diffraction
2Å resolution

Crystal structure of the third RCC1-like domain of HERC1

Source organism: Homo sapiens
Entry authors: Dong A, Hu J, Li Y, Walker JR, Bountra C, Arrowsmith CH, Edwards AM, Tong Y, Structural Genomics Consortium (SGC)

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)
Entry contents:
1 distinct polypeptide molecule
Probable E3 ubiquitin-protein ligase HERC1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 404 amino acids
Theoretical weight: 42.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q15751 (Residues: 3975-4360; Coverage: 8%)
Gene name: HERC1
Sequence domains: Regulator of chromosome condensation (RCC1) repeat
Structure domains: Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 53.383Å b: 70.902Å c: 105.549Å
α: 70.93° β: 81.26° γ: 90.84°
R R work R free
0.182 0.181 0.221
Expression system: Escherichia coli BL21(DE3)