1TBQ

CRYSTAL STRUCTURE OF INSECT DERIVED DOUBLE DOMAIN KAZAL INHIBITOR RHODNIIN IN COMPLEX WITH THROMBIN

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
R	0004867	molecular_function	serine-type endopeptidase inhibitor activity
R	0005576	cellular_component	extracellular region
R	0030414	molecular_function	peptidase inhibitor activity
S	0004867	molecular_function	serine-type endopeptidase inhibitor activity
S	0005576	cellular_component	extracellular region
S	0030414	molecular_function	peptidase inhibitor activity

Functional Information from PROSITE/UniProt

site_id	PS00282
Number of Residues	24
Details	KAZAL_1 Kazal serine protease inhibitors family signature. CphalHrvCgSdgetYsnpCtlnC

Chain	Residue	Details
R	CYS8-CYS31

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. DAceGDSGGPFV

Chain	Residue	Details
H	ASP189-VAL200

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|Ref.4