1ELE

STRUCTURAL ANALYSIS OF THE ACTIVE SITE OF PORCINE PANCREATIC ELASTASE BASED ON THE X-RAY CRYSTAL STRUCTURES OF COMPLEXES WITH TRIFLUOROACETYL-DIPEPTIDE-ANILIDE INHIBITORS

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0006508	biological_process	proteolysis
E	0006954	biological_process	inflammatory response
E	0008233	molecular_function	peptidase activity
E	0008236	molecular_function	serine-type peptidase activity
E	0016787	molecular_function	hydrolase activity
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 0QN E 256

Chain	Residue
E	HIS60
E	SER222
E	PHE223
E	VAL224
E	ARG226
E	HOH666
E	GLU65
E	LEU66
E	THR67
E	ALA104
E	CYS199
E	GLN200
E	SER203
E	THR221

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 280

Chain	Residue
E	GLU74
E	ASN76
E	GLN79
E	ASN81
E	GLU84
E	HOH327

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 290

Chain	Residue
E	GLY133
E	ARG151
E	ARG240
E	SER242
E	ALA243
E	HOH432

---

site_id	CAT
Number of Residues	3
Details	CATALYTIC SITE

Chain	Residue
E	HIS60
E	ASP108
E	SER203

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	MET56-CYS61

---

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

Chain	Residue	Details
E	SER197-HIS208

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	237
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	1
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"4578945","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"5415110","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"5415110","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7656008","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ELA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ELB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ELC","evidenceCode":"ECO:0007744"}]}

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	HIS60
E	ASP108

---

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

Chain	Residue	Details
E	GLY204
E	SER203

---

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

Chain	Residue	Details
E	GLY201
E	SER203

---

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

Chain	Residue	Details
E	HIS60
E	SER203
E	ASP108

---

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

Chain	Residue	Details
E	GLY204
E	HIS60
E	SER203
E	ASP108

---

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

Chain	Residue	Details
E	GLY201
E	HIS60
E	SER203
E	ASP108

---

site_id	CSA7
Number of Residues	5
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
E	GLY201
E	HIS60
E	SER222
E	SER203
E	ASP108

---