5w87

X-ray diffraction
2.2Å resolution

Crystal structure of the C-terminal lobe of the human HERC6 HECT domain

Released:
Source organism: Homo sapiens
Entry authors: WANG Y, BELLESIS AG, ROYER WE, SPRATT DE

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-184879 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable E3 ubiquitin-protein ligase HERC6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 121 amino acids
Theoretical weight: 14.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IVU3 (Residues: 902-1022; Coverage: 12%)
Gene name: HERC6
Sequence domains: HECT-domain (ubiquitin-transferase)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: R3
Unit cell:
a: 74.579Å b: 74.579Å c: 114.89Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.211 0.244
Expression system: Escherichia coli