4A6L

beta-tryptase inhibitor

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	16
Details	BINDING SITE FOR RESIDUE P43 A 1263

Chain	Residue
A	GLN105
A	TRP233
A	GLY234
A	GLU235
A	GLY237
A	HOH2053
C	ASP64
C	TYR102
A	TYR181
A	ILE193
A	ASP207
A	SER208
A	CYS209
A	GLN210
A	SER213
A	VAL231

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE P43 B 1263

Chain	Residue
B	GLN105
B	TYR181
B	ILE193
B	ASP207
B	SER208
B	CYS209
B	SER213
B	VAL231
B	TRP233
B	GLY234
B	GLU235
B	GLY237
B	HOH2086
D	ASP64
D	TYR102

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE P43 C 1263

Chain	Residue
A	ASP64
A	TYR102
C	GLN105
C	TYR181
C	ILE193
C	ASP207
C	SER208
C	CYS209
C	GLN210
C	SER213
C	VAL231
C	TRP233
C	GLY234
C	GLU235
C	GLY237
C	ARG243
C	GLY245
C	HOH2080

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE P43 D 1263

Chain	Residue
B	ASP64
B	TYR102
D	GLN105
D	TYR181
D	ILE193
D	ASP207
D	SER208
D	SER213
D	VAL231
D	TRP233
D	GLY234
D	GLU235
D	GLY237
D	GLY245
D	HOH2077

---

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	LEU55-CYS60

---

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

Chain	Residue	Details
A	ASP207-VAL218

---

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	HIS59
D	HIS59
D	ASP109
D	SER213
A	ASP109
A	SER213
B	HIS59
B	ASP109
B	SER213
C	HIS59
C	ASP109
C	SER213

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	LYS120
A	ASN222
B	LYS120
B	ASN222
C	LYS120
C	ASN222
D	LYS120
D	ASN222

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P21845

Chain	Residue	Details
A	TYR82
B	TYR82
C	TYR82
D	TYR82

---