› 2y6u

X-ray diffraction
1.9Å resolution

Peroxisomal alpha-beta-hydrolase Lpx1 (Yor084w) from Saccharomyces cerevisiae (crystal form II)

Released:
DOI: 10.2210/pdb2y6u/pdb
PDB entry 2y6u coloured by chain, front view.
PDB entry 2y6u coloured by chain, side view.
PDB entry 2y6u coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
The unusual extended C-terminal helix of the peroxisomal α/β-hydrolase Lpx1 is involved in dimer contacts but dispensable for dimerization.
Thoms S, Hofhuis J, Thöing C, Gärtner J, Niemann HH
J Struct Biol 175 362-71 (2011)
PMID: 21741480

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171355 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peroxisomal membrane protein LPX1 Chain: A
Molecule details ›
Chain: A
Length: 398 amino acids
Theoretical weight: 45.21 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q12405 (Residues: 1-387; Coverage: 100%)
Gene names: LPX1, YOR084W, YOR3120W
Sequence domains: Alpha/beta hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
2 modified residues:
Ligand CME 1 x CME
Ligand CSO 4 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P3221
Unit cell:
a: 87.156Å b: 87.156Å c: 125.52Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 0.153 0.179
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Import of proteins into peroxisomes: piggybacking to a new home away from home.
Thoms S. (2015)
11 other articles

1 mention without citation

Zearalenone lactonohydrolase activity in Hypocreales and its evolutionary relationships within the epoxide hydrolase subset of a/b-hydrolases.
Popiel et al. (2014)