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7m3q

X-ray diffraction
2.5Å resolution

Structure of the Smurf2 HECT Domain with a High Affinity Ubiquitin Variant (UbV)

Released:
Model geometry
Fit model/data
Source organism: Homo sapiens
Entry authors: Chowdhury A, Singer AU, Ogunjimi AA, Teyra J, Zhang W, Sicheri F, Sidhu SS

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptorprotein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-158841 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase SMURF2 Chain: A
Molecule details ›
Chain: A
Length: 387 amino acids
Theoretical weight: 45.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HAU4 (Residues: 366-748; Coverage: 51%)
Gene name: SMURF2
Sequence domains: HECT-domain (ubiquitin-transferase)
Ubiquitin Chain: B
Molecule details ›
Chain: B
Length: 98 amino acids
Theoretical weight: 11.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P62987 (Residues: 1-74; Coverage: 58%)
Gene names: UBA52, UBCEP2
Sequence domains: Ubiquitin family

Ligands and Environments

No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 201.53Å b: 72.068Å c: 48.813Å
α: 90° β: 94.607° γ: 90°
R-values:
R R work R free
0.204 0.203 0.235
Expression system: Escherichia coli BL21(DE3)