6ww3

X-ray diffraction
2.1Å resolution

Crystal structure of HERC2 ZZ domain in complex with SUMO1 tail

Released:
Source organism: Homo sapiens

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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-131990 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase HERC2; Small ubiquitin-related modifier 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 60 amino acids
Theoretical weight: 6.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63165 (Residues: 2-7; Coverage: 6%)
  • Canonical: O95714 (Residues: 2702-2755; Coverage: 1%)
Gene names: HERC2, OK/SW-cl.43, SMT3C, SMT3H3, SUMO1, UBL1
Sequence domains: Zinc finger, ZZ type

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 41.882Å b: 47.262Å c: 55.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.227
Expression system: Escherichia coli