2WWP

Crystal structure of the human lipocalin-type prostaglandin D synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001516	biological_process	prostaglandin biosynthetic process
A	0004667	molecular_function	prostaglandin-D synthase activity
A	0005501	molecular_function	retinoid binding
A	0005504	molecular_function	fatty acid binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005791	cellular_component	rough endoplasmic reticulum
A	0005794	cellular_component	Golgi apparatus
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006693	biological_process	prostaglandin metabolic process
A	0010467	biological_process	gene expression
A	0016853	molecular_function	isomerase activity
A	0019371	biological_process	cyclooxygenase pathway
A	0031965	cellular_component	nuclear membrane
A	0036094	molecular_function	small molecule binding
A	0043303	biological_process	mast cell degranulation
A	0045187	biological_process	regulation of circadian sleep/wake cycle, sleep
A	0046457	biological_process	prostanoid biosynthetic process
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0051384	biological_process	response to glucocorticoid
A	0070062	cellular_component	extracellular exosome
A	2000255	biological_process	negative regulation of male germ cell proliferation
B	0001516	biological_process	prostaglandin biosynthetic process
B	0004667	molecular_function	prostaglandin-D synthase activity
B	0005501	molecular_function	retinoid binding
B	0005504	molecular_function	fatty acid binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005791	cellular_component	rough endoplasmic reticulum
B	0005794	cellular_component	Golgi apparatus
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006693	biological_process	prostaglandin metabolic process
B	0010467	biological_process	gene expression
B	0016853	molecular_function	isomerase activity
B	0019371	biological_process	cyclooxygenase pathway
B	0031965	cellular_component	nuclear membrane
B	0036094	molecular_function	small molecule binding
B	0043303	biological_process	mast cell degranulation
B	0045187	biological_process	regulation of circadian sleep/wake cycle, sleep
B	0046457	biological_process	prostanoid biosynthetic process
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0051384	biological_process	response to glucocorticoid
B	0070062	cellular_component	extracellular exosome
B	2000255	biological_process	negative regulation of male germ cell proliferation

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL A 1185

Chain	Residue
A	LEU159

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SCN A 1186

Chain	Residue
A	GLN36
A	ASP37

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SCN B 1183

Chain	Residue
B	GLN36
B	ASP37

---

Functional Information from PROSITE/UniProt

site_id	PS00213
Number of Residues	14
Details	LIPOCALIN Lipocalin signature. NFQqdKFLGRWFSA

Chain	Residue	Details
A	ASN33-ALA46

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"20667974","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GalNAc...) serine","evidences":[{"source":"PubMed","id":"23234360","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

---