Top Level Name

  ⌊ Superfamily (core) Glutathione Transferase (cytosolic)

    ⌊ Subgroup AMPS (cytGST): Alpha-, Mu-, Pi-, and Sigma-like

  AMPS.1

  ⌊ FunctionalDomain similar to Alpha, Mu, Pi, and Sigma class cytGSTs (ID 55701)

Superfamily Assignment Evidence Code(s) ISS
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Homo sapiens Taxon ID: 9606 7657457 NP_055300.1 (RefSeq) PRP URP
synthetic construct Taxon ID: 32630 649108099 AIC51217.1 (Genbank)
n/a 396988617 AFN90229.1 (Genbank)
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Uniprot

Protein NameAccessionEC Number Identifier
Hematopoietic prostaglandin D synthase O60760 HPGDS_HUMAN (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 199 | Length of Functional Domain: 199

1       10        20        30        40        50        60

MPNYKLTYFNMRGRAEIIRYIFAYLDIQYEDHRIEQADWPEIKSTLPFGKIPILEVDGLT
LHQSLAIARYLTKNTDLAGNTEMEQCHVDAIVDTLDDFMSCFPWAEKKQDVKEQMFNELL
TYNAPHLMQDLDTYLGGREWLIGNSVTWADFYWEICSTTLLVFKPDLLDNHPRLVTLRKK
VQAIPAVANWIKRRPQTKL
This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. The Superfamily domain, when present, is shown using underlining. In many cases the functional domain is the full-length sequence.
Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues

Subgroup CAR This EFD conserves 1/1 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
8 Tyr (Y) side chain None -- ISS PubMed:9074797

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Links
3KXO An Orally Active Inhibitor Bound At The Active Site Of Hpgds Glutathione-Requiring Prostaglandin D Synthase 10 2.1 Glutathione
(2 more ⇓)
CSA • PDB • PDBSum
2VCX Complex Structure Of Prostaglandin D2 Synthase At 2.1A. Glutathione-Requiring Prostaglandin D Synthase 10 2.1 Phenyl-5-(1H-Pyrazol-3-Yl)-1,3-Thiazole
(2 more ⇓)
CSA • PDB • PDBSum
2VCZ Complex Structure Of Prostaglandin D2 Synthase At 1.95A. Glutathione-Requiring Prostaglandin D Synthase 10 1.95 3-(4-Nitrophenyl)-1H-Pyrazole • Glutathione CSA • PDB • PDBSum
2VD0 Complex Structure Of Prostaglandin D2 Synthase At 2.2A. Glutathione-Requiring Prostaglandin D Synthase 10 2.2 2-{[(2E)-3-(3,4-Dimethoxyphenyl)Prop-2-Enoyl] Amino}Benzoic Acid
(2 more ⇓)
CSA • PDB • PDBSum
2VD1 Complex Structure Of Prostaglandin D2 Synthase At 2.25A. Glutathione-Requiring Prostaglandin D Synthase 10 2.25 4-{[4-(4-Fluoro-3-Methylphenyl)-1,3-Thiazol-2-Yl]Amino}-2-Hydroxybenzoic Acid
(2 more ⇓)
CSA • PDB • PDBSum
2VCW Complex Structure Of Prostaglandin D2 Synthase At 1.95A. Glutathione-Requiring Prostaglandin D Synthase 10 1.95 1-Phenyl-1H-Pyrazole-4-Carboxylic Acid • Glutathione CSA • PDB • PDBSum
2VCQ Complex Structure Of Prostaglandin D2 Synthase At 1.95A. Glutathione-Requiring Prostaglandin D Synthase 10 1.95 3-Phenyl-5-(1H-Pyrazol-3-Yl)Isoxazole • Glutathione CSA • PDB • PDBSum
4EC0 Crystal Structure Of Hh-Pgds With Water Displacing Inhibitor Hematopoietic Prostaglandin D Synthase 10 1.85 Glutathione
(2 more ⇓)
CSA • PDB • PDBSum
4EDZ Crystal Structure Of Hh-Pgds With Water Displacing Inhibitor Hematopoietic Prostaglandin D Synthase 10 2.0 Glutathione
(2 more ⇓)
CSA • PDB • PDBSum
4EE0 Crystal Structure Of Hh-Pgds With Water Displacing Inhibitor Hematopoietic Prostaglandin D Synthase 10 1.75 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
4EDY Crystal Structure Of Hh-Pgds With Water Displacing Inhibitor Hematopoietic Prostaglandin D Synthase 10 1.72 Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
5AIS Complex Of Human Hematopoietic Prostagandin D2 Synthase (Hh-Pgds) In Complex With An Active Site Inhibitor. Hematopoietic Prostaglandin D Synthase 10 1.85 4-(Dimethylamino)-N-[5-(1H-Indol-4-Yl) Pyridin-3-Yl]Butanamide
(2 more ⇓)
CSA • PDB • PDBSum
3EE2 Structure Of Human Prostaglandin D-Synthase (Hgsts1-1) In Complex With Nocodazole Glutathione-Requiring Prostaglandin D Synthase 11 1.91 Glutathione
(2 more ⇓)
CSA • PDB • PDBSum
1IYI Crystal Structure Of Hematopoietic Prostaglandin D Synthase Hematopoietic Prostagladin D Synthase 10 1.8 Calcium Ion • Glutathione CSA • PDB • PDBSum
1IYH Crystal Structure Of Hematopoietic Prostaglandin D Synthase Hematopoietic Prostagladin D Synthase 10 1.7 Magnesium Ion • Glutathione CSA • PDB • PDBSum
2CVD Crystal Structure Analysis Of Human Hematopoietic Prostaglandin D Synthase Complexed With Hql-79 Glutathione-Requiring Prostaglandin D Synthase 10 1.45 Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
1V40 First Inhibitor Complex Structure Of Human Hematopoietic Prostaglandin D Synthase Glutathione-Requiring Prostaglandin D Synthase 10 1.9 Magnesium Ion
(3 more ⇓)
CSA • PDB • PDBSum
3VI5 Human Hematopoietic Prostaglandin D Synthase Inhibitor Complex Structures Hematopoietic Prostaglandin D Synthase 10 2.0 Yes Glutathione
(3 more ⇓)
CSA • PDB • PDBSum
3VI7 Human Hematopoietic Prostaglandin D Synthase Inhibitor Complex Structures Hematopoietic Prostaglandin D Synthase 10 2.0 Yes Glutathione
(2 more ⇓)
CSA • PDB • PDBSum
5AIX Complex Of Human Hematopoietic Prostagandin D2 Synthase (Hh-Pgds) In Complex With An Active Site Inhibitor. Hematopoietic Prostaglandin D Synthase 10 2.1 6-(3-Methoxyphenyl)-N-[1-(2,2,2-Trifluoroethyl)Piperidin-4-Yl]Pyridine-3-Carboxamide
(2 more ⇓)
CSA • PDB • PDBSum
5AIV Complex Of Human Hematopoietic Prostagandin D2 Synthase (Hh-Pgds) In Complex With An Active Site Inhibitor. Hematopoietic Prostaglandin D Synthase 10 2.04 3-(1H-Indol-4-Yl)-N-(3-Methoxypropyl)-1,2,4-Oxadiazole-5-Carboxamide
(2 more ⇓)
CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via UniProtKB.

Curation History

Time Change Annotation Old Value New Value
May 3, 2014, 6:39 a.m. update curation agent smashiya setDomainBoundaries.py
update domain end position 199 193
update domain start position 1 3
Aug. 16, 2016, 8:33 a.m. update domain end position 193 199
update domain start position 3 1
EC number assigned by UniProtKB accession ID.