6NVB

Crystal structure of the inhibitor-free form of the serine protease kallikrein-4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0006508	biological_process	proteolysis
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	0030141	cellular_component	secretory granule
A	0031214	biological_process	biomineral tissue development
A	0046872	molecular_function	metal ion binding
A	0051604	biological_process	protein maturation
A	0097186	biological_process	amelogenesis
B	0004252	molecular_function	serine-type endopeptidase activity
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0006508	biological_process	proteolysis
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	0030141	cellular_component	secretory granule
B	0031214	biological_process	biomineral tissue development
B	0046872	molecular_function	metal ion binding
B	0051604	biological_process	protein maturation
B	0097186	biological_process	amelogenesis
C	0004252	molecular_function	serine-type endopeptidase activity
C	0005576	cellular_component	extracellular region
C	0005615	cellular_component	extracellular space
C	0006508	biological_process	proteolysis
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	0030141	cellular_component	secretory granule
C	0031214	biological_process	biomineral tissue development
C	0046872	molecular_function	metal ion binding
C	0051604	biological_process	protein maturation
C	0097186	biological_process	amelogenesis
D	0004252	molecular_function	serine-type endopeptidase activity
D	0005576	cellular_component	extracellular region
D	0005615	cellular_component	extracellular space
D	0006508	biological_process	proteolysis
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	0030141	cellular_component	secretory granule
D	0031214	biological_process	biomineral tissue development
D	0046872	molecular_function	metal ion binding
D	0051604	biological_process	protein maturation
D	0097186	biological_process	amelogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue GOL A 301

Chain	Residue
A	ASP189
A	GLY226
A	HOH427
A	HOH473
A	SER190
A	LYS217
A	PRO219
A	CYS220
A	GLY220
A	GLN221
A	VAL224
A	PRO225

---

site_id	AC2
Number of Residues	12
Details	binding site for residue GOL B 301

Chain	Residue
B	ASP189
B	SER190
B	LYS217
B	PRO219
B	CYS220
B	GLY220
B	GLN221
B	VAL224
B	PRO225
B	GLY226
B	HOH494
B	HOH531

---

site_id	AC3
Number of Residues	6
Details	binding site for residue GOL B 302

Chain	Residue
A	ASP109
B	VAL47
B	HIS48
B	PRO49
B	SER120
B	SER122

---

site_id	AC4
Number of Residues	7
Details	binding site for residue SO4 B 303

Chain	Residue
B	HIS57
B	ASN192
B	GLY193
B	SER195
B	HOH407
B	HOH529
B	HOH613

---

site_id	AC5
Number of Residues	11
Details	binding site for residue GOL C 301

Chain	Residue
C	ASP189
C	SER190
C	LYS217
C	CYS220
C	GLY220
C	GLN221
C	VAL224
C	PRO225
C	GLY226
C	HOH447
C	HOH479

---

site_id	AC6
Number of Residues	11
Details	binding site for residue GOL D 301

Chain	Residue
D	ASP189
D	SER190
D	LYS217
D	CYS220
D	GLY220
D	GLN221
D	VAL224
D	PRO225
D	GLY226
D	HOH440
D	HOH444

---

site_id	AC7
Number of Residues	7
Details	binding site for residue GOL D 302

Chain	Residue
C	ASP109
D	VAL47
D	HIS48
D	PRO49
D	SER120
D	SER122
D	HOH560

---

site_id	AC8
Number of Residues	7
Details	binding site for residue SO4 D 303

Chain	Residue
D	HIS57
D	ASN192
D	GLY193
D	SER195
D	HOH422
D	HOH471
D	HOH519

---

Functional Information from PROSITE/UniProt

site_id	PS00134
Number of Residues	6
Details	TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LSAAHC

Chain	Residue	Details
A	LEU53-CYS58

---

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

Chain	Residue	Details
A	ASP189-ILE200

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	884
Details	Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"16950394","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16950394","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---