6nnq

X-ray diffraction
2.62Å resolution

Non-covalent structure of SENP1 in complex with SUMO2

Released:
Source organism: Homo sapiens
Primary publication:
Noncovalent structure of SENP1 in complex with SUMO2.
Acta Crystallogr F Struct Biol Commun 75 332-339 (2019)
PMID: 31045562

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-157327 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Sentrin-specific protease 1 Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 26.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P0U3 (Residues: 421-644; Coverage: 35%)
Gene name: SENP1
Sequence domains: Ulp1 protease family, C-terminal catalytic domain
Structure domains: Adenoviral Proteinase; Chain A
Small ubiquitin-related modifier 3 Chain: B
Molecule details ›
Chain: B
Length: 78 amino acids
Theoretical weight: 8.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P55854 (Residues: 15-92; Coverage: 76%)
Gene names: SMT3A, SMT3H1, SUMO3
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P4322
Unit cell:
a: 98.732Å b: 98.732Å c: 101.805Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.229 0.277
Expression system: Escherichia coli