3PB1

Crystal Structure of a Michaelis Complex between Plasminogen Activator Inhibitor-1 and Urokinase-type Plasminogen Activator

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004252	molecular_function	serine-type endopeptidase activity
E	0006508	biological_process	proteolysis
I	0001525	biological_process	angiogenesis
I	0002020	molecular_function	protease binding
I	0004866	molecular_function	endopeptidase inhibitor activity
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity
I	0005102	molecular_function	signaling receptor binding
I	0005515	molecular_function	protein binding
I	0005576	cellular_component	extracellular region
I	0005615	cellular_component	extracellular space
I	0005886	cellular_component	plasma membrane
I	0009617	biological_process	response to bacterium
I	0010757	biological_process	negative regulation of plasminogen activation
I	0014912	biological_process	negative regulation of smooth muscle cell migration
I	0030194	biological_process	positive regulation of blood coagulation
I	0030195	biological_process	negative regulation of blood coagulation
I	0030336	biological_process	negative regulation of cell migration
I	0030414	molecular_function	peptidase inhibitor activity
I	0031012	cellular_component	extracellular matrix
I	0031093	cellular_component	platelet alpha granule lumen
I	0032757	biological_process	positive regulation of interleukin-8 production
I	0033629	biological_process	negative regulation of cell adhesion mediated by integrin
I	0035491	biological_process	positive regulation of leukotriene production involved in inflammatory response
I	0042730	biological_process	fibrinolysis
I	0045766	biological_process	positive regulation of angiogenesis
I	0045861	biological_process	negative regulation of proteolysis
I	0048260	biological_process	positive regulation of receptor-mediated endocytosis
I	0050729	biological_process	positive regulation of inflammatory response
I	0050820	biological_process	positive regulation of coagulation
I	0050829	biological_process	defense response to Gram-negative bacterium
I	0051918	biological_process	negative regulation of fibrinolysis
I	0061044	biological_process	negative regulation of vascular wound healing
I	0061045	biological_process	negative regulation of wound healing
I	0070062	cellular_component	extracellular exosome
I	0070495	biological_process	negative regulation of thrombin-activated receptor signaling pathway
I	0071222	biological_process	cellular response to lipopolysaccharide
I	0090026	biological_process	positive regulation of monocyte chemotaxis
I	0090399	biological_process	replicative senescence
I	0097180	cellular_component	serine protease inhibitor complex
I	0097187	biological_process	dentinogenesis
I	1901331	biological_process	positive regulation of odontoblast differentiation
I	1902042	biological_process	negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
I	1904090	cellular_component	peptidase inhibitor complex
I	2000098	biological_process	negative regulation of smooth muscle cell-matrix adhesion
I	2000352	biological_process	negative regulation of endothelial cell apoptotic process
I	2001045	biological_process	negative regulation of integrin-mediated signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 1

Chain	Residue
E	SER48
E	PRO49
E	CYS50
E	TRP51
I	ARG30
I	HOH497

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 E 2

Chain	Residue
E	SER125
E	MET126
E	ARG239

---

Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. ISATHC

Chain	Residue	Details
E	ILE53-CYS58

---

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. IIIDRPFLFvV

Chain	Residue	Details
I	ILE352-VAL362

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Site: {"description":"Reactive bond"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	245
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"9151681","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000026"}

Chain

Residue

Details

---