Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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STRUCTURE OF SERINE PROTEINASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0007596	biological_process	blood coagulation
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005509	molecular_function	calcium ion binding
B	0006508	biological_process	proteolysis
B	0007596	biological_process	blood coagulation
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005576	cellular_component	extracellular region
C	0006508	biological_process	proteolysis
C	0007596	biological_process	blood coagulation
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005509	molecular_function	calcium ion binding
D	0006508	biological_process	proteolysis
D	0007596	biological_process	blood coagulation
E	0004252	molecular_function	serine-type endopeptidase activity
E	0005576	cellular_component	extracellular region
E	0006508	biological_process	proteolysis
E	0007596	biological_process	blood coagulation
F	0004252	molecular_function	serine-type endopeptidase activity
F	0005509	molecular_function	calcium ion binding
F	0006508	biological_process	proteolysis
F	0007596	biological_process	blood coagulation
G	0004252	molecular_function	serine-type endopeptidase activity
G	0005576	cellular_component	extracellular region
G	0006508	biological_process	proteolysis
G	0007596	biological_process	blood coagulation
H	0004252	molecular_function	serine-type endopeptidase activity
H	0005509	molecular_function	calcium ion binding
H	0006508	biological_process	proteolysis
H	0007596	biological_process	blood coagulation
R	0004867	molecular_function	serine-type endopeptidase inhibitor activity
R	0005576	cellular_component	extracellular region
R	0030133	cellular_component	transport vesicle
R	0030414	molecular_function	peptidase inhibitor activity
R	0031410	cellular_component	cytoplasmic vesicle
R	0035821	biological_process	modulation of process of another organism
R	0090729	molecular_function	toxin activity
S	0004867	molecular_function	serine-type endopeptidase inhibitor activity
S	0005576	cellular_component	extracellular region
S	0030133	cellular_component	transport vesicle
S	0030414	molecular_function	peptidase inhibitor activity
S	0031410	cellular_component	cytoplasmic vesicle
S	0035821	biological_process	modulation of process of another organism
S	0090729	molecular_function	toxin activity
T	0004867	molecular_function	serine-type endopeptidase inhibitor activity
T	0005576	cellular_component	extracellular region
T	0030133	cellular_component	transport vesicle
T	0030414	molecular_function	peptidase inhibitor activity
T	0031410	cellular_component	cytoplasmic vesicle
T	0035821	biological_process	modulation of process of another organism
T	0090729	molecular_function	toxin activity
U	0004867	molecular_function	serine-type endopeptidase inhibitor activity
U	0005576	cellular_component	extracellular region
U	0030133	cellular_component	transport vesicle
U	0030414	molecular_function	peptidase inhibitor activity
U	0031410	cellular_component	cytoplasmic vesicle
U	0035821	biological_process	modulation of process of another organism
U	0090729	molecular_function	toxin activity

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
B	LEU53-CYS58

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

Chain	Residue	Details
B	ASP189-VAL200

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1016
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	88
Details	Region: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1975","firstPage":"25","lastPage":"46","publisher":"Leiden University Press","address":"Leiden","bookName":"Boerhaave symposium on prothrombin and related coagulation factors","editors":["Hemker H.C.","Veltkamp J.J."],"authors":["Magnusson S.","Sottrup-Jensen L.","Petersen T.E.","Claeys H."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	208
Details	Domain: {"description":"BPTI/Kunitz inhibitor 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8947023","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	220
Details	Domain: {"description":"BPTI/Kunitz inhibitor 2","evidences":[{"source":"PubMed","id":"8947023","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Region: {"description":"Linker"}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP102
B	SER195
B	GLY193
B	HIS57

site_id	CSA10
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	ASP102
D	SER195
D	HIS57

site_id	CSA11
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
F	ASP102
F	SER195
F	HIS57

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ASP102
H	SER195
H	HIS57

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	ASP102
D	SER195
D	GLY193
D	HIS57

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
F	ASP102
F	SER195
F	GLY193
F	HIS57

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ASP102
H	SER195
H	GLY193
H	HIS57

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

Chain	Residue	Details
B	ASP102
B	SER195
B	HIS57
B	GLY196

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

Chain	Residue	Details
D	ASP102
D	SER195
D	HIS57
D	GLY196

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
F	ASP102
F	SER195
F	HIS57
F	GLY196

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ASP102
H	SER195
H	HIS57
H	GLY196

site_id	CSA9
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP102
B	SER195
B	HIS57

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)