8VGI

CryoEM structure of tryptase in complex with engineered conformationally rigid anti-tryptase Fab E104.v1.2DS

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	0006952	biological_process	defense response
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0016787	molecular_function	hydrolase activity
A	0022617	biological_process	extracellular matrix disassembly
A	0031012	cellular_component	extracellular matrix
A	0042802	molecular_function	identical protein binding
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006508	biological_process	proteolysis
B	0006952	biological_process	defense response
B	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0016787	molecular_function	hydrolase activity
B	0022617	biological_process	extracellular matrix disassembly
B	0031012	cellular_component	extracellular matrix
B	0042802	molecular_function	identical protein binding
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0006508	biological_process	proteolysis
C	0006952	biological_process	defense response
C	0008233	molecular_function	peptidase activity
C	0008236	molecular_function	serine-type peptidase activity
C	0016787	molecular_function	hydrolase activity
C	0022617	biological_process	extracellular matrix disassembly
C	0031012	cellular_component	extracellular matrix
C	0042802	molecular_function	identical protein binding
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0006508	biological_process	proteolysis
D	0006952	biological_process	defense response
D	0008233	molecular_function	peptidase activity
D	0008236	molecular_function	serine-type peptidase activity
D	0016787	molecular_function	hydrolase activity
D	0022617	biological_process	extracellular matrix disassembly
D	0031012	cellular_component	extracellular matrix
D	0042802	molecular_function	identical protein binding

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

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

Chain	Residue	Details
A	ASP189-VAL200

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site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH

Chain	Residue	Details
F	TYR198-HIS204
E	TYR192-HIS198

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: Charge relay system

Chain	Residue	Details
A	HIS57
D	HIS57
D	ASP102
D	SER195
A	ASP102
A	SER195
B	HIS57
B	ASP102
B	SER195
C	HIS57
C	ASP102
C	SER195

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site_id	SWS_FT_FI2
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN113
B	ASN113
C	ASN113
D	ASN113

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site_id	SWS_FT_FI3
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
A	ASN204
B	ASN204
C	ASN204
D	ASN204

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