1EST

THE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE STRUCTURE OF ALPHA-CHYMOTRYPSIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 A 246

Chain	Residue
A	ARG230

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE TOS A 247

Chain	Residue
A	CYS191
A	GLN192
A	GLY193
A	SER195
A	SER214

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site_id	CAT
Number of Residues	3
Details

Chain	Residue
A	HIS57
A	ASP102
A	SER195

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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
A	MET53-CYS58

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

Chain	Residue	Details
A	SER189-HIS200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Charge relay system => ECO:0000269|PubMed:4578945, ECO:0000269|PubMed:5415110

Chain	Residue	Details
A	HIS57

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000269|PubMed:5415110

Chain	Residue	Details
A	ASP102
A	SER195

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:7656008, ECO:0007744|PDB:1ELA, ECO:0007744|PDB:1ELB, ECO:0007744|PDB:1ELC

Chain	Residue	Details
A	GLU70
A	ASN72
A	GLN75
A	GLU80

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