› 4ory

X-ray diffraction
1.8Å resolution

Three-dimensional structure of the C65A-K59A double mutant of Human lipocalin-type Prostaglandin D Synthase holo, second crystal form

Released:
DOI: 10.2210/pdb4ory/pdb
PDB entry 4ory coloured by chain, front view.
PDB entry 4ory coloured by chain, side view.
PDB entry 4ory 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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154342 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prostaglandin-H2 D-isomerase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 190 amino acids
Theoretical weight: 20.96 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

1 bound ligand:
Ligand PEU 2 x PEU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P41
Unit cell:
a: 67.378Å b: 67.378Å c: 287.673Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.249
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