Structure of PDB 1pd2 Chain 2

Receptor sequence
>1pd22 (length=199) Species: 10116 (Rattus norvegicus) [Search protein sequence]
MPNYKLLYFNMRGRAEIIRYIFAYLDIKYEDHRIEQADWPKIKPTLPFGK
IPVLEVEGLTLHQSLAIARYLTKNTDLAGKTELEQCQVDAVVDTLDDFMS
LFPWAEENQDLKERTFNDLLTRQAPHLLKDLDTYLGDKEWFIGNYVTWAD
FYWDICSTTLLVLKPDLLGIYPRLVSLRNKVQAIPAISAWILKRPQTKL
3D structure
PDB1pd2 Cloning and crystal structure of hematopoietic prostaglandin D synthase.
Chain2
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y8 R14 W104
Catalytic site (residue number reindexed from 1) Y8 R14 W104
Enzyme Commision number 2.5.1.18: glutathione transferase.
5.3.99.2: prostaglandin-D synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GSH 2 R14 W39 K43 K50 I51 Q63 S64 R14 W39 K43 K50 I51 Q63 S64
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004364 glutathione transferase activity
GO:0004667 prostaglandin-D synthase activity
GO:0005509 calcium ion binding
GO:0016740 transferase activity
GO:0016853 isomerase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0001516 prostaglandin biosynthetic process
GO:0006693 prostaglandin metabolic process
GO:0009624 response to nematode
GO:0010269 response to selenium ion
GO:2000255 negative regulation of male germ cell proliferation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1pd2, PDBe:1pd2, PDBj:1pd2
PDBsum1pd2
PubMed9323136
UniProtO35543|HPGDS_RAT Hematopoietic prostaglandin D synthase (Gene Name=Hpgds)

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