3F9C

Crystal structure of human plasma platelet activating factor acetylhydrolase covalently inhibited by diisopropylfluorophosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003847	molecular_function	1-alkyl-2-acetylglycerophosphocholine esterase activity
A	0005515	molecular_function	protein binding
A	0005543	molecular_function	phospholipid binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006629	biological_process	lipid metabolic process
A	0009395	biological_process	phospholipid catabolic process
A	0016042	biological_process	lipid catabolic process
A	0016486	biological_process	peptide hormone processing
A	0016787	molecular_function	hydrolase activity
A	0016788	molecular_function	hydrolase activity, acting on ester bonds
A	0034362	cellular_component	low-density lipoprotein particle
A	0034364	cellular_component	high-density lipoprotein particle
A	0034374	biological_process	low-density lipoprotein particle remodeling
A	0034440	biological_process	lipid oxidation
A	0034441	biological_process	plasma lipoprotein particle oxidation
A	0034638	biological_process	phosphatidylcholine catabolic process
A	0046469	biological_process	platelet activating factor metabolic process
A	0047499	molecular_function	calcium-independent phospholipase A2 activity
A	0050729	biological_process	positive regulation of inflammatory response
A	0062234	biological_process	platelet activating factor catabolic process
A	0090026	biological_process	positive regulation of monocyte chemotaxis
B	0003847	molecular_function	1-alkyl-2-acetylglycerophosphocholine esterase activity
B	0005515	molecular_function	protein binding
B	0005543	molecular_function	phospholipid binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006629	biological_process	lipid metabolic process
B	0009395	biological_process	phospholipid catabolic process
B	0016042	biological_process	lipid catabolic process
B	0016486	biological_process	peptide hormone processing
B	0016787	molecular_function	hydrolase activity
B	0016788	molecular_function	hydrolase activity, acting on ester bonds
B	0034362	cellular_component	low-density lipoprotein particle
B	0034364	cellular_component	high-density lipoprotein particle
B	0034374	biological_process	low-density lipoprotein particle remodeling
B	0034440	biological_process	lipid oxidation
B	0034441	biological_process	plasma lipoprotein particle oxidation
B	0034638	biological_process	phosphatidylcholine catabolic process
B	0046469	biological_process	platelet activating factor metabolic process
B	0047499	molecular_function	calcium-independent phospholipase A2 activity
B	0050729	biological_process	positive regulation of inflammatory response
B	0062234	biological_process	platelet activating factor catabolic process
B	0090026	biological_process	positive regulation of monocyte chemotaxis

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DFP A 473

Chain	Residue
A	GLY152
A	LEU153
A	HIS272
A	SER273
A	PHE274
A	HIS351
A	GLN352

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DFP B 473

Chain	Residue
B	SER273
B	PHE274
B	HIS351
B	GLN352
B	GLY152
B	LEU153

---

Functional Information from PROSITE/UniProt

site_id	PS00120
Number of Residues	10
Details	LIPASE_SER Lipases, serine active site. IAVIGHSFGG

Chain	Residue	Details
A	ILE267-GLY276

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"18784071","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU10037","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18784071","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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