Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2F9N

Crystal Structure of the Recombinant Human Alpha I Tryptase Mutant K192Q/D216G in Complex with Leupeptin

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	0008236	molecular_function	serine-type peptidase activity
A	0022617	biological_process	extracellular matrix disassembly
A	0042802	molecular_function	identical protein binding
A	0062023	cellular_component	collagen-containing extracellular matrix
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	0008236	molecular_function	serine-type peptidase activity
B	0022617	biological_process	extracellular matrix disassembly
B	0042802	molecular_function	identical protein binding
B	0062023	cellular_component	collagen-containing extracellular matrix
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	0008236	molecular_function	serine-type peptidase activity
C	0022617	biological_process	extracellular matrix disassembly
C	0042802	molecular_function	identical protein binding
C	0062023	cellular_component	collagen-containing extracellular matrix
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	0008236	molecular_function	serine-type peptidase activity
D	0022617	biological_process	extracellular matrix disassembly
D	0042802	molecular_function	identical protein binding
D	0062023	cellular_component	collagen-containing extracellular matrix

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. DScqGDSGGPLV

Chain	Residue	Details
A	ASP189-VAL200

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

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

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

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	HIS57

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	SER195
B	GLY193

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	SER195
C	GLY193

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	SER195
D	GLY193

site_id	CSA13
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	HIS57
A	GLY196

site_id	CSA14
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	CSA15
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	HIS57
C	GLY196

site_id	CSA16
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	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP102
B	SER195
B	HIS57

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	HIS57

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

Chain	Residue	Details
D	ASP102
D	SER195
D	HIS57

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

Chain	Residue	Details
A	ASP102
A	SER195
A	GLY193
A	HIS57

site_id	CSA6
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	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP102
C	SER195
C	GLY193
C	HIS57

site_id	CSA8
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	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	SER195
A	GLY193

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)