PDBe 2iy0

X-ray diffraction
2.77Å resolution

SENP1 (mutant) SUMO1 RanGAP

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 trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Sentrin-specific protease 1 Chain: A
Molecule details ›
Chain: A
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 Chain: B
Molecule details ›
Chain: B
Length: 82 amino acids
Theoretical weight: 9.52 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
Ran GTPase-activating protein 1 Chain: C
Molecule details ›
Chain: C
Length: 156 amino acids
Theoretical weight: 17.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P46060 (Residues: 432-587; Coverage: 27%)
Gene names: KIAA1835, RANGAP1, SD
Structure domains: Ran-GTPase activating protein 1, C-terminal domain

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: 83.38Å b: 83.38Å c: 148.044Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.279
Expression system: Escherichia coli