X-ray diffraction
1.5Å resolution

Crystal Structure of Phosphatidic acid Transporter Ups1/Mdm35 Void of Bound Phospholipid from Saccharomyces Cerevisiae at 1.5 Angstroms Resolution

Primary publication:
Molecular mechanism of mitochondrial phosphatidate transfer by Ups1.
Commun Biol 3 468 (2020)
PMID: 32843686

Function and Biology Details

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Mitochondrial distribution and morphology protein 35; Protein UPS1, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 283 amino acids
Theoretical weight: 32.35 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
  • Canonical: Q05776 (Residues: 1-175; Coverage: 100%)
  • Canonical: O60200 (Residues: 1-86; Coverage: 100%)
Gene names: MDM35, UPS1, YKL053C-A, YLR193C
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 118.563Å b: 68.29Å c: 105.137Å
α: 90° β: 102.1° γ: 90°
R R work R free
0.166 0.164 0.202
Expression system: Escherichia coli