› 4os0

X-ray diffraction
1.75Å resolution

Three-dimensional structure of the C65A-W54F double mutant of Human lipocalin-type Prostaglandin D Synthase apo-form

Released:
DOI: 10.2210/pdb4os0/pdb
PDB entry 4os0 coloured by chain, front view.
PDB entry 4os0 coloured by chain, side view.
PDB entry 4os0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High-resolution structures of mutants of residues that affect access to the ligand-binding cavity of human lipocalin-type prostaglandin D synthase.
Perduca M, Bovi M, Bertinelli M, Bertini E, Destefanis L, Carrizo ME, Capaldi S, Monaco HL
Acta Crystallogr D Biol Crystallogr 70 2125-38 (2014)
PMID: 25084332

Function and Biology Details

Reaction catalysed: 
(5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-154342 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostaglandin-H2 D-isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 190 amino acids
Theoretical weight: 20.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P41222 (Residues: 1-190; Coverage: 100%)
Gene names: PDS, PTGDS
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P1
Unit cell:
a: 41.622Å b: 45.87Å c: 48.26Å
α: 69.4° β: 77.67° γ: 65.32°
R-values:
R R work R free
0.198 0.196 0.233
Expression system: Escherichia coli

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Citations

1 review citation

Biochemical and Structural Characteristics, Gene Regulation, Physiological, Pathological and Clinical Features of Lipocalin-Type Prostaglandin D2 Synthase as a Multifunctional Lipocalin.
Urade Y. (2021)
1 other article