1PPF

X-RAY CRYSTAL STRUCTURE OF THE COMPLEX OF HUMAN LEUKOCYTE ELASTASE (PMN ELASTASE) AND THE THIRD DOMAIN OF THE TURKEY OVOMUCOID INHIBITOR

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0000122	biological_process	negative regulation of transcription by RNA polymerase II
E	0001878	biological_process	response to yeast
E	0002020	molecular_function	protease binding
E	0002438	biological_process	acute inflammatory response to antigenic stimulus
E	0002523	biological_process	leukocyte migration involved in inflammatory response
E	0002812	biological_process	biosynthetic process of antibacterial peptides active against Gram-negative bacteria
E	0003714	molecular_function	transcription corepressor activity
E	0004175	molecular_function	endopeptidase activity
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005615	cellular_component	extracellular space
E	0005737	cellular_component	cytoplasm
E	0005794	cellular_component	Golgi apparatus
E	0005829	cellular_component	cytosol
E	0006508	biological_process	proteolysis
E	0006874	biological_process	intracellular calcium ion homeostasis
E	0006909	biological_process	phagocytosis
E	0008201	molecular_function	heparin binding
E	0008233	molecular_function	peptidase activity
E	0008236	molecular_function	serine-type peptidase activity
E	0009411	biological_process	response to UV
E	0009986	cellular_component	cell surface
E	0016787	molecular_function	hydrolase activity
E	0017053	cellular_component	transcription repressor complex
E	0019955	molecular_function	cytokine binding
E	0022617	biological_process	extracellular matrix disassembly
E	0030141	cellular_component	secretory granule
E	0030163	biological_process	protein catabolic process
E	0031012	cellular_component	extracellular matrix
E	0031410	cellular_component	cytoplasmic vesicle
E	0032496	biological_process	response to lipopolysaccharide
E	0032682	biological_process	negative regulation of chemokine production
E	0032717	biological_process	negative regulation of interleukin-8 production
E	0032757	biological_process	positive regulation of interleukin-8 production
E	0035578	cellular_component	azurophil granule lumen
E	0035580	cellular_component	specific granule lumen
E	0042742	biological_process	defense response to bacterium
E	0043406	biological_process	positive regulation of MAP kinase activity
E	0045335	cellular_component	phagocytic vesicle
E	0048661	biological_process	positive regulation of smooth muscle cell proliferation
E	0050728	biological_process	negative regulation of inflammatory response
E	0050778	biological_process	positive regulation of immune response
E	0050832	biological_process	defense response to fungus
E	0050900	biological_process	leukocyte migration
E	0050922	biological_process	negative regulation of chemotaxis
E	0070062	cellular_component	extracellular exosome
E	0070269	biological_process	pyroptotic inflammatory response
E	0070945	biological_process	neutrophil-mediated killing of gram-negative bacterium
E	0070947	biological_process	neutrophil-mediated killing of fungus
E	1903238	biological_process	positive regulation of leukocyte tethering or rolling
I	0004867	molecular_function	serine-type endopeptidase inhibitor activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	MET53-CYS58

---

site_id	PS00135
Number of Residues	12
Details	TRYPSIN_SER Serine proteases, trypsin family, serine active site. GVcfGDSGSPLV

Chain	Residue	Details
E	GLY189-VAL200

---

site_id	PS00282
Number of Residues	23
Details	KAZAL_1 Kazal serine protease inhibitors family signature. CtleyRplCgSdnktYgnkCnf.C

Chain	Residue	Details
I	CYS16-CYS38

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	217
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"2911584","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"26274980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3550808","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3550808","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	54
Details	Domain: {"description":"Kazal-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00798","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Reactive bond 3 for chymotrypsin, elastase, proteases A and B, and subtilisin"}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	HIS57

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	SER195
E	GLY196

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	SER195
E	GLY193

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	HIS57

---

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	GLY193
E	HIS57

---

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	ASP102
E	SER195
E	HIS57
E	GLY196

---