PDBe 5iaa

X-ray diffraction
1.85Å resolution

Crystal structure of human UBA5 in complex with UFM1

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-like modifier-activating enzyme 5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 290 amino acids
Theoretical weight: 32.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9GZZ9 (Residues: 57-346; Coverage: 72%)
Gene names: UBA5, UBE1DC1
Structure domains: NAD(P)-binding Rossmann-like Domain
Ubiquitin-fold modifier 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 83 amino acids
Theoretical weight: 8.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61960 (Residues: 1-83; Coverage: 98%)
Gene names: BM-002, C13orf20, UFM1
Sequence domains: Ubiquitin fold modifier 1 protein
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.3
Spacegroup: P3221
Unit cell:
a: 138.081Å b: 138.081Å c: 99.178Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.187 0.206
Expression system: Escherichia coli