PDBe 4w5v

X-ray diffraction
2.5Å resolution

Crystal structure of Human SUMO E2-conjugating enzyme (Ubc9) in complex with E1-activating enzyme (Uba2) ubiquitin fold domain (Ufd)

Released:
Source organism: Homo sapiens
Entry authors: Boucher LE, Reiter KH, Matunis MJ, Bosch J

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: 163 amino acids
Theoretical weight: 18.44 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
SUMO-activating enzyme subunit 2 Chain: B
Molecule details ›
Chain: B
Length: 122 amino acids
Theoretical weight: 13.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBT2 (Residues: 445-561; Coverage: 18%)
Gene names: HRIHFB2115, SAE2, UBA2, UBLE1B
Sequence domains: Ubiquitin/SUMO-activating enzyme ubiquitin-like domain
Structure domains: Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2
Unit cell:
a: 161.273Å b: 35.272Å c: 58.672Å
α: 90° β: 96.69° γ: 90°
R-values:
R R work R free
0.224 0.221 0.283
Expression system: Escherichia coli