1ORF

The Oligomeric Structure of Human Granzyme A Reveals the Molecular Determinants of Substrate Specificity

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001772	cellular_component	immunological synapse
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	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0006915	biological_process	apoptotic process
A	0006955	biological_process	immune response
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0031640	biological_process	killing of cells of another organism
A	0042803	molecular_function	protein homodimerization activity
A	0043065	biological_process	positive regulation of apoptotic process
A	0044194	cellular_component	cytolytic granule
A	0051603	biological_process	obsolete proteolysis involved in protein catabolic process
A	0051604	biological_process	protein maturation
A	0070269	biological_process	pyroptotic inflammatory response
A	0140507	biological_process	granzyme-mediated programmed cell death signaling pathway
A	1902483	biological_process	cytotoxic T cell pyroptotic cell death

Functional Information from PDB Data

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU53-CYS58

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

Chain	Residue	Details
A	ASP189-LEU200

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	230
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	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"12819769","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12819770","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"12819769","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12819770","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32299851","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

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

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

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

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

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