Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3O19

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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OLA A 200
ChainResidue
ALEU27
ATHR119
ATYR121
APLM201
ALYS31
ALEU34
ASER53
APHE55
AARG64
AMET66
ATYR79
AMET117

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLM A 201
ChainResidue
AASN23
ASER24
ATRP26
ALEU51
AMET66
ATYR79
ATYR88
ASER105
APRO111
AASP114
AASP114
APHE115
AMET117
ATYR121
AOLA200
AHOH287
AHOH341

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFQqdKFLGRWFSA
ChainResidueDetails
AASN5-ALA18

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:20667974
ChainResidueDetails
AALA37

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:23234360
ChainResidueDetails
ASER1

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:8336134
ChainResidueDetails
AASN23

site_idSWS_FT_FI4
Number of Residues1
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
AASN50

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon