Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BDH

Human Kallikrein 4 complex with zinc and p-aminobenzamidine

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	4
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	HIS25
A	GLU77
B	GLU74
B	ASP75

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PBZ B 301

Chain	Residue
B	LYS217
B	CYS220
B	ASP189
B	SER190
B	SER195
B	SER214
B	GLY216

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PBZ C 302

Chain	Residue
C	ASP189
C	SER190
C	SER195
C	VAL213
C	SER214
C	PHE215
C	CYS220

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PBZ A 303

Chain	Residue
A	ASP189
A	SER190
A	ASN192
A	SER195
A	VAL213
A	CYS220
A	HOH404
A	HOH432

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PBZ D 304

Chain	Residue
D	ASP189
D	SER190
D	CYS191
D	SER195
D	VAL213
D	PHE215
D	GLY216
D	CYS220

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

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	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
B	ASP102
B	SER195
B	GLY193
B	HIS57

site_id	CSA11
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	CSA12
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	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	SER195
A	ALA100
A	HIS57
A	GLY196

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

Chain	Residue	Details
B	SER195
B	ALA100
B	HIS57
B	GLY196

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

Chain	Residue	Details
C	SER195
C	ALA100
C	HIS57
C	GLY196

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
D	SER195
D	ALA100
D	HIS57
D	GLY196

site_id	CSA9
Number of Residues	4
Details	Annotated By Reference To The Literature 1a0j

Chain	Residue	Details
A	ASP102
A	SER195
A	GLY193
A	HIS57

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