PDBe 2iy1

X-ray diffraction
2.46Å resolution

SENP1 (mutant) full length SUMO1

Released:
Source organism: Homo sapiens
Primary publication:
SUMO protease SENP1 induces isomerization of the scissile peptide bond.
Nat. Struct. Mol. Biol. 13 1069-77 (2006)
PMID: 17099698

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Sentrin-specific protease 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 226 amino acids
Theoretical weight: 26.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q9P0U3 (Residues: 419-644; Coverage: 35%)
Gene name: SENP1
Sequence domains: Ulp1 protease family, C-terminal catalytic domain
Structure domains: Adenoviral Proteinase; Chain A
Small ubiquitin-related modifier 1 Chains: B, D
Molecule details ›
Chains: B, D
Length: 83 amino acids
Theoretical weight: 9.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P63165 (Residues: 20-101; Coverage: 81%)
Gene names: OK/SW-cl.43, SMT3C, SMT3H3, SUMO1, UBL1
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P43212
Unit cell:
a: 141.232Å b: 141.232Å c: 98.964Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.249 0.281
Expression system: Escherichia coli