PDBe 1y8x

X-ray diffraction
2.4Å resolution

Structural basis for recruitment of Ubc12 by an E2-binding domain in NEDD8's E1

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
NEDD8-conjugating enzyme Ubc12 Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 18.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61081 (Residues: 27-183; Coverage: 86%)
Gene names: UBC12, UBE2M
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
NEDD8-activating enzyme E1 catalytic subunit Chain: B
Molecule details ›
Chain: B
Length: 98 amino acids
Theoretical weight: 10.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TBC4 (Residues: 368-463; Coverage: 21%)
Gene names: UBA3, UBE1C
Sequence domains: E2 binding domain
Structure domains: Ubiquitin-like 2 activating enzyme e1b. Chain: B, domain 3

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 40.606Å b: 61.518Å c: 125.938Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.242 0.259
Expression system: Escherichia coli