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3O2Y

Structure-function analysis of human L-Prostaglandin D Synthase bound with fatty acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0001516biological_processprostaglandin biosynthetic process
A0004667molecular_functionprostaglandin-D synthase activity
A0005501molecular_functionretinoid binding
A0005504molecular_functionfatty acid binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005791cellular_componentrough endoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006693biological_processprostaglandin metabolic process
A0010467biological_processgene expression
A0016020cellular_componentmembrane
A0016853molecular_functionisomerase activity
A0019371biological_processcyclooxygenase pathway
A0031965cellular_componentnuclear membrane
A0036094molecular_functionsmall molecule binding
A0043303biological_processmast cell degranulation
A0045187biological_processregulation of circadian sleep/wake cycle, sleep
A0048471cellular_componentperinuclear region of cytoplasm
A0051384biological_processresponse to glucocorticoid
A0070062cellular_componentextracellular exosome
A2000255biological_processnegative regulation of male germ cell proliferation
B0001516biological_processprostaglandin biosynthetic process
B0004667molecular_functionprostaglandin-D synthase activity
B0005501molecular_functionretinoid binding
B0005504molecular_functionfatty acid binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005791cellular_componentrough endoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006693biological_processprostaglandin metabolic process
B0010467biological_processgene expression
B0016020cellular_componentmembrane
B0016853molecular_functionisomerase activity
B0019371biological_processcyclooxygenase pathway
B0031965cellular_componentnuclear membrane
B0036094molecular_functionsmall molecule binding
B0043303biological_processmast cell degranulation
B0045187biological_processregulation of circadian sleep/wake cycle, sleep
B0048471cellular_componentperinuclear region of cytoplasm
B0051384biological_processresponse to glucocorticoid
B0070062cellular_componentextracellular exosome
B2000255biological_processnegative regulation of male germ cell proliferation
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE OLA A 200
ChainResidue
ASER45
AMET145
ATHR147
APLM201
AHOH272
ALEU48
ALEU55
ALYS59
ALEU62
AMET64
ASER81
APHE83
AMET94

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLM A 201
ChainResidue
ASER52
ALEU79
AMET94
ATYR116
ASER133
APHE143
AMET145
ATYR149
AOLA200
AHOH237
AHOH256
AHOH272

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OLA B 202
ChainResidue
BLEU55
BLYS59
BLEU62
BMET64
BPHE83
BMET94
BMET145
BTHR147
BTYR149
BPLM203

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLM B 203
ChainResidue
AASP142
BASN51
BSER52
BTRP54
BLEU55
BMET94
BSER133
BPHE143
BMET145
BOLA202
BHOH221
BHOH228

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL B 252
ChainResidue
BTHR73
BASN78

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFQqdKFLGRWFSA
ChainResidueDetails
AASN33-ALA46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:20667974
ChainResidueDetails
AALA65
BALA65

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:23234360
ChainResidueDetails
ASER29
BSER29

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:8336134
ChainResidueDetails
AASN51
BASN51

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:8336134
ChainResidueDetails
AASN78
BASN78

218853

PDB entries from 2024-04-24

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