PDBe 3pyc

X-ray diffraction
1.96Å resolution

Crystal structure of human SMURF1 C2 domain

Released:
Source organism: Homo sapiens
Entry authors: Li X, Li P

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase SMURF1 Chain: A
Molecule details ›
Chain: A
Length: 132 amino acids
Theoretical weight: 14.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HCE7 (Residues: 13-140; Coverage: 17%)
Gene names: KIAA1625, SMURF1
Sequence domains: C2 domain
Structure domains: C2 domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P212121
Unit cell:
a: 30.959Å b: 47.048Å c: 91.266Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.241
Expression system: Escherichia coli