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4IMO

Crystal structure of wild type human Lipocalin PGDS in complex with substrate analog U44069

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
A0031965cellular_componentnuclear membrane
A0036094molecular_functionsmall molecule binding
A0043303biological_processmast cell degranulation
A0045187biological_processregulation of circadian sleep/wake cycle, sleep
A0046457biological_processprostanoid biosynthetic process
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 Residues10
DetailsBINDING SITE FOR RESIDUE PWZ A 201
ChainResidue
AARG42
APHE143
ATRP54
ALYS66
AVAL68
ATHR80
ATRP112
ATYR116
APRO139
AGLY140

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PWZ A 202
ChainResidue
ASER45
ASER67
ASER81
ATYR107
ASER109
ATRP112
ATYR149
ASCN203
AHOH317
AHOH327
AHOH382

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN A 203
ChainResidue
AGLN36
AASP37
AARG85
APWZ202

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 204
ChainResidue
APRO32
ATYR128
ALEU159
ALYS162
AHOH350

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 Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20667974","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"23234360","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8336134","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22171320","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8336134","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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