3O2Y

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

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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OLA A 200

Chain	Residue
A	SER45
A	MET145
A	THR147
A	PLM201
A	HOH272
A	LEU48
A	LEU55
A	LYS59
A	LEU62
A	MET64
A	SER81
A	PHE83
A	MET94

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLM A 201

Chain	Residue
A	SER52
A	LEU79
A	MET94
A	TYR116
A	SER133
A	PHE143
A	MET145
A	TYR149
A	OLA200
A	HOH237
A	HOH256
A	HOH272

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OLA B 202

Chain	Residue
B	LEU55
B	LYS59
B	LEU62
B	MET64
B	PHE83
B	MET94
B	MET145
B	THR147
B	TYR149
B	PLM203

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLM B 203

Chain	Residue
A	ASP142
B	ASN51
B	SER52
B	TRP54
B	LEU55
B	MET94
B	SER133
B	PHE143
B	MET145
B	OLA202
B	HOH221
B	HOH228

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 252

Chain	Residue
B	THR73
B	ASN78

---

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

---