3O22

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	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
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	0016020	cellular_component	membrane
A	0016853	molecular_function	isomerase activity
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OLA A 200

Chain	Residue
A	LEU55
A	HOH287
A	LYS59
A	LEU62
A	SER81
A	PHE83
A	ARG92
A	MET145
A	PLM192
A	PLM201

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PLM A 201

Chain	Residue
A	ASN51
A	SER52
A	LEU55
A	MET94
A	TYR116
A	SER133
A	ASP142
A	ASP142
A	PHE143
A	MET145
A	OLA191
A	PLM192
A	OLA200

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OLA A 191

Chain	Residue
A	LEU48
A	LEU55
A	LYS59
A	LEU62
A	MET64
A	SER81
A	THR147
A	TYR149
A	LEU180
A	PLM192
A	HOH194
A	PLM201
A	HOH287

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLM A 192

Chain	Residue
A	MET94
A	TYR116
A	VAL118
A	SER133
A	PRO139
A	ASP142
A	MET145
A	OLA191
A	OLA200
A	PLM201
A	HOH287
A	HOH338

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASN33-ALA46

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:20667974

Chain	Residue	Details
A	ALA65

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	CARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:23234360

Chain	Residue	Details
A	SER29

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:8336134

Chain	Residue	Details
A	ASN51

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	CARBOHYD: 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

Chain	Residue	Details
A	ASN78

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