› 7nvk

X-ray diffraction
2.65Å resolution

Crystal structure of UBA5 fragment fused to the N-terminus of UFC1

Released:
DOI: 10.2210/pdb7nvk/pdb
PDB entry 7nvk coloured by chain, front view.
PDB entry 7nvk coloured by chain, side view.
PDB entry 7nvk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for UFM1 transfer from UBA5 to UFC1.
Kumar M, Padala P, Fahoum J, Hassouna F, Tsaban T, Zoltsman G, Banerjee S, Cohen-Kfir E, Dessau M, Rosenzweig R, Isupov MN, Schueler-Furman O, Wiener R
OpenAccess logo Nat Commun 12 5708 (2021)
PMID: 34588452

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190463 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-fold modifier-conjugating enzyme 1; Ubiquitin-like modifier-activating enzyme 5 Chain: AAA
Molecule details ›
Chain: AAA
Length: 226 amino acids
Theoretical weight: 25.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9GZZ9 (Residues: 347-404; Coverage: 14%)
  • Canonical: Q9Y3C8 (Residues: 1-167; Coverage: 100%)
Gene names: CGI-126, HSPC155, UBA5, UBE1DC1, UFC1
Sequence domains: Ubiquitin-fold modifier-conjugating enzyme 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P64
Unit cell:
a: 84.63Å b: 84.63Å c: 60.77Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.216 0.264
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

A non-canonical scaffold-type E3 ligase complex mediates protein UFMylation.
Peter et al. (2022)
8 more