› 5ia7

X-ray diffraction
2Å resolution

Crystal structure of Ubiquitin fold modifier 1 (Ufm1)

Released:
DOI: 10.2210/pdb5ia7/pdb
PDB entry 5ia7 coloured by chain, front view.
PDB entry 5ia7 coloured by chain, side view.
PDB entry 5ia7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Novel insights into the interaction of UBA5 with UFM1 via a UFM1-interacting sequence.
Padala P, Oweis W, Mashahreh B, Soudah N, Cohen-Kfir E, Todd EA, Berndsen CE, Wiener R
Sci Rep 7 508 (2017)
PMID: 28360427

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-158470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-fold modifier 1 Chains: A, B
Molecule details ›
Chains: A, B
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P212121
Unit cell:
a: 45.282Å b: 56.73Å c: 64.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.23
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The UFMylation System in Proteostasis and Beyond.
Gerakis et al. (2019)
2 more

4 mentions without citation

Chromatin Regulation through Ubiquitin and Ubiquitin-like Histone Modifications.
Vaughan et al. (2021)
3 more