2grq

X-ray diffraction
1.7Å resolution

Crystal Structure of human RanGAP1-Ubc9-D127A

Released:
Source organism: Homo sapiens
Primary publication:
Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway.
Nat Struct Mol Biol 13 491-9 (2006)
PMID: 16732283

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-155412 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SUMO-conjugating enzyme UBC9 Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63279 (Residues: 1-158; Coverage: 100%)
Gene names: UBC9, UBCE9, UBE2I
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
Ran GTPase-activating protein 1 Chain: B
Molecule details ›
Chain: B
Length: 170 amino acids
Theoretical weight: 18.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P46060 (Residues: 419-587; Coverage: 29%)
Gene names: KIAA1835, RANGAP1, SD
Sequence domains: RanGAP1 C-terminal domain
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: P1
Unit cell:
a: 39.284Å b: 44.813Å c: 61.012Å
α: 72.35° β: 71.89° γ: 75.35°
R-values:
R R work R free
0.189 0.189 0.205
Expression system: Escherichia coli