PDBe 2grr

X-ray diffraction
1.3Å resolution

Crystal Structure of human RanGAP1-Ubc9-D127S

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)
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: 18.29 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
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 24-ID-C
Spacegroup: P1
Unit cell:
a: 39.15Å b: 44.675Å c: 61.013Å
α: 72.61° β: 71.72° γ: 75.35°
R-values:
R R work R free
0.201 0.201 0.222
Expression system: Escherichia coli