Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3BSQ

Crystal structure of human kallikrein 7 produced as a secretion protein in E.coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001533	cellular_component	cornified envelope
A	0002803	biological_process	positive regulation of antibacterial peptide production
A	0004222	molecular_function	metalloendopeptidase activity
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	0008544	biological_process	epidermis development
A	0022617	biological_process	extracellular matrix disassembly
A	0030141	cellular_component	secretory granule
A	0097209	cellular_component	epidermal lamellar body
B	0001533	cellular_component	cornified envelope
B	0002803	biological_process	positive regulation of antibacterial peptide production
B	0004222	molecular_function	metalloendopeptidase activity
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	0008544	biological_process	epidermis development
B	0022617	biological_process	extracellular matrix disassembly
B	0030141	cellular_component	secretory granule
B	0097209	cellular_component	epidermal lamellar body
C	0001533	cellular_component	cornified envelope
C	0002803	biological_process	positive regulation of antibacterial peptide production
C	0004222	molecular_function	metalloendopeptidase activity
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	0008544	biological_process	epidermis development
C	0022617	biological_process	extracellular matrix disassembly
C	0030141	cellular_component	secretory granule
C	0097209	cellular_component	epidermal lamellar body

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 1

Chain	Residue
A	LYS58
A	SER84
A	ARG86

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 5

Chain	Residue
A	HIS56
A	ASN188
A	GLY189
A	SER191

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 7

Chain	Residue
A	GLY199
A	THR200
A	TRP29
A	ARG118

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 8

Chain	Residue
A	PRO159
A	ASN172
A	LYS226
C	GLN38

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 9

Chain	Residue
A	LYS58
A	SER82
A	LYS83
A	SER84

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 13

Chain	Residue
A	SER91
A	THR92
A	GLN93

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 2

Chain	Residue
B	SO411
B	LYS58
B	SER84
B	PHE85
B	ARG86

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 10

Chain	Residue
B	SO415
B	HIS56
B	ASN188
B	GLY189
B	SER191

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 11

Chain	Residue
B	SO42
B	LYS58
B	SER82
B	SER84

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 12

Chain	Residue
B	ARG49
B	SER106
B	GLN107

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 14

Chain	Residue
B	GLN93
B	THR94
B	HIS95
B	LEU169

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 15

Chain	Residue
B	SO410
B	ALA186
B	CYS187
B	ASN188
B	GLY208

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 3

Chain	Residue
C	LYS58
C	SER84
C	PHE85
C	ARG86

site_id	BC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 4

Chain	Residue
C	LYS58
C	LYS83
C	SER84

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 6

Chain	Residue
C	HIS56
C	ASN188
C	GLY189
C	SER191

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 239

Chain	Residue
C	LYS83
C	PHE85
C	HIS237

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	LEU52-CYS57

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

Chain	Residue	Details
A	ASN185-VAL196

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	ACT_SITE: Charge relay system => ECO:0000269\|PubMed:17909180

Chain	Residue	Details
A	HIS56
A	ASP98
A	SER191
B	HIS56
B	ASP98
B	SER191
C	HIS56
C	ASP98
C	SER191

site_id	SWS_FT_FI2
Number of Residues	3
Details	SITE: Major binding site for inhibitory zinc or copper

Chain	Residue	Details
A	HIS95
B	HIS95
C	HIS95

site_id	SWS_FT_FI3
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN232
B	ASN232
C	ASN232

Catalytic Information from CSA

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

Chain	Residue	Details
A	ASP98
A	HIS56
A	SER191

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

Chain	Residue	Details
A	GLY189
A	SER191

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

Chain	Residue	Details
B	GLY189
B	SER191

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

Chain	Residue	Details
C	GLY189
C	SER191

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	GLY192
A	SER191

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	GLY192
B	SER191

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	GLY192
C	SER191

site_id	CSA16
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP98
A	GLY189
A	HIS56
A	SER191

site_id	CSA17
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP98
B	GLY189
B	HIS56
B	SER191

site_id	CSA18
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
C	ASP98
C	GLY189
C	HIS56
C	SER191

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

Chain	Residue	Details
B	ASP98
B	HIS56
B	SER191

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

Chain	Residue	Details
C	ASP98
C	HIS56
C	SER191

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	GLY192
A	ASP98
A	HIS56
A	SER191

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

Chain	Residue	Details
B	GLY192
B	ASP98
B	HIS56
B	SER191

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

Chain	Residue	Details
C	GLY192
C	ASP98
C	HIS56
C	SER191

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP98
A	HIS56

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

Chain	Residue	Details
B	ASP98
B	HIS56

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

Chain	Residue	Details
C	ASP98
C	HIS56

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