Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2FWW

human beta-tryptase II complexed with 4-piperidinebutyrate to make acylenzyme

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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity
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	0008236	molecular_function	serine-type peptidase activity
D	0062023	cellular_component	collagen-containing extracellular matrix

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE C1R A 999

Chain	Residue
A	ASP189
A	HOH1005
A	SER190
A	CYS191
A	GLN192
A	GLY193
A	ASP194
A	SER195
A	TRP215
A	GLY226

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE C1R B 998

Chain	Residue
B	ASP189
B	SER190
B	CYS191
B	GLN192
B	GLY193
B	ASP194
B	SER195
B	TRP215
B	GLY219
B	GLY226
B	HOH1085

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE C1R C 997

Chain	Residue
C	ASP189
C	SER190
C	CYS191
C	GLN192
C	GLY193
C	ASP194
C	SER195
C	VAL213
C	TRP215
C	GLY219
C	GLY226

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE C1R D 996

Chain	Residue
D	ASP189
D	SER190
D	CYS191
D	GLN192
D	GLY193
D	ASP194
D	SER195
D	TRP215
D	GLY219
D	GLY226
D	HOH1055

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 => ECO:0000255\|PROSITE-ProRule:PRU00274

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	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P21845

Chain	Residue	Details
A	TYR75
B	TYR75
C	TYR75
D	TYR75

site_id	SWS_FT_FI3
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

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
C	SER195
C	GLY193

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

Chain	Residue	Details
D	SER195
D	GLY193

site_id	CSA12
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	CSA13
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	CSA14
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	CSA15
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	CSA16
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	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	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	SER195
A	GLY193

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

Chain	Residue	Details
B	SER195
B	GLY193

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