1BTH

STRUCTURE OF THROMBIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR

Functional Information from GO Data

Chain	GOid	namespace	contents
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
J	0004252	molecular_function	serine-type endopeptidase activity
J	0005576	cellular_component	extracellular region
J	0006508	biological_process	proteolysis
J	0007596	biological_process	blood coagulation
K	0004252	molecular_function	serine-type endopeptidase activity
K	0005509	molecular_function	calcium ion binding
K	0006508	biological_process	proteolysis
K	0007596	biological_process	blood coagulation
L	0004252	molecular_function	serine-type endopeptidase activity
L	0005576	cellular_component	extracellular region
L	0006508	biological_process	proteolysis
L	0007596	biological_process	blood coagulation
P	0004867	molecular_function	serine-type endopeptidase inhibitor activity
Q	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. LTAAHC

Chain	Residue	Details
H	LEU53-CYS58

---

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

Chain	Residue	Details
H	ASP189-VAL200

---

site_id	PS00280
Number of Residues	19
Details	BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCrakrnnFksaedC

Chain	Residue	Details
P	PHE33-CYS51

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	44
Details	Region: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Charge relay system"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	100
Details	Domain: {"description":"BPTI/Kunitz inhibitor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00031","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Site: {"description":"Reactive bond for trypsin"}

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
H	ASP102
H	SER195
H	GLY193
H	HIS57

---

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

Chain	Residue	Details
K	ASP102
K	SER195
K	GLY193
K	HIS57

---

site_id	CSA3
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	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
K	ASP102
K	SER195
K	HIS57
K	GLY196

---

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
H	ASP102
H	SER195
H	HIS57

---

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
K	ASP102
K	SER195
K	HIS57

---