7q41

X-ray diffraction
3.01Å resolution

Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with DXDKDED motif of ubiquitin-protein ligase E3A (E6AP)

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:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-221181 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-protein ligase E3A Chains: B, D, F
Molecule details ›
Chains: B, D, F
Length: 15 amino acids
Theoretical weight: 1.72 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q05086 (Residues: 183-197; Coverage: 2%)
Gene names: E6AP, EPVE6AP, HPVE6A, UBE3A
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: SLS BEAMLINE X06DA
Spacegroup: P43212
Unit cell:
a: 108.952Å b: 108.952Å c: 243.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.255
Expression systems:
  • Not provided
  • Escherichia coli