PDBe 2io2

X-ray diffraction
2.9Å resolution

Crystal structure of human Senp2 in complex with RanGAP1-SUMO-1

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates.
Nat. Struct. Mol. Biol. 13 1060-8 (2006)
PMID: 17099700

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero 12-mer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Sentrin-specific protease 2 Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 27.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q9HC62 (Residues: 364-589; Coverage: 38%)
Gene names: KIAA1331, SENP2
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: 9.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P63165 (Residues: 18-97; Coverage: 79%)
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: 172 amino acids
Theoretical weight: 18.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P46060 (Residues: 418-587; Coverage: 29%)
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: APS BEAMLINE 31-ID
Spacegroup: P6422
Unit cell:
a: 163.96Å b: 163.96Å c: 77.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.268 0.268 0.301
Expression system: Escherichia coli