Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5B2G

Crystal structure of human claudin-4 in complex with C-terminal fragment of Clostridium perfringens enterotoxin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0005198	molecular_function	structural molecule activity
A	0005923	cellular_component	bicellular tight junction
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis
B	0005576	cellular_component	extracellular region
C	0003796	molecular_function	lysozyme activity
C	0005198	molecular_function	structural molecule activity
C	0005923	cellular_component	bicellular tight junction
C	0009253	biological_process	peptidoglycan catabolic process
C	0016020	cellular_component	membrane
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0016998	biological_process	cell wall macromolecule catabolic process
C	0030430	cellular_component	host cell cytoplasm
C	0031640	biological_process	killing of cells of another organism
C	0042742	biological_process	defense response to bacterium
C	0044659	biological_process	viral release from host cell by cytolysis
D	0005576	cellular_component	extracellular region
E	0003796	molecular_function	lysozyme activity
E	0005198	molecular_function	structural molecule activity
E	0005923	cellular_component	bicellular tight junction
E	0009253	biological_process	peptidoglycan catabolic process
E	0016020	cellular_component	membrane
E	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
E	0016998	biological_process	cell wall macromolecule catabolic process
E	0030430	cellular_component	host cell cytoplasm
E	0031640	biological_process	killing of cells of another organism
E	0042742	biological_process	defense response to bacterium
E	0044659	biological_process	viral release from host cell by cytolysis
F	0005576	cellular_component	extracellular region
G	0003796	molecular_function	lysozyme activity
G	0005198	molecular_function	structural molecule activity
G	0005923	cellular_component	bicellular tight junction
G	0009253	biological_process	peptidoglycan catabolic process
G	0016020	cellular_component	membrane
G	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
G	0016998	biological_process	cell wall macromolecule catabolic process
G	0030430	cellular_component	host cell cytoplasm
G	0031640	biological_process	killing of cells of another organism
G	0042742	biological_process	defense response to bacterium
G	0044659	biological_process	viral release from host cell by cytolysis
H	0005576	cellular_component	extracellular region

Functional Information from PROSITE/UniProt

site_id	PS01346
Number of Residues	16
Details	CLAUDIN Claudin family signature. GLWmnCvvqstgqm.QC

Chain	Residue	Details
A	GLY1212-CYS1227

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
C	GLU1011
A	GLU1011
E	GLU1011
G	GLU1011

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|HAMAP-Rule:MF_04110, ECO:0000269\|PubMed:1892846, ECO:0000269\|PubMed:3382407, ECO:0000269\|PubMed:7831309, ECO:0000269\|PubMed:8266098

Chain	Residue	Details
A	ASP1020
C	ASP1020
E	ASP1020
G	ASP1020

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:8266098

Chain	Residue	Details
C	LEU1032
C	PHE1104
E	LEU1032
A	LEU1032
A	PHE1104
E	PHE1104
G	LEU1032
G	PHE1104

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000303\|PubMed:7831309

Chain	Residue	Details
C	ASN1132
A	SER1117
A	ASN1132
C	SER1117
E	SER1117
E	ASN1132
G	SER1117
G	ASN1132

site_id	SWS_FT_FI5
Number of Residues	80
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
A	MET1164-GLN1170
A	LYS1266-THR1280
C	MET1-GLN7
C	LYS103-THR117
E	MET1164-GLN1170
E	LYS1266-THR1280
G	MET1164-GLN1170
G	LYS1266-THR1280

site_id	SWS_FT_FI6
Number of Residues	320
Details	TRANSMEM: Helical => ECO:0000255

Chain	Residue	Details
A	VAL1171-PRO1191
A	ALA1245-GLY1265
A	MET1281-TRP1301
A	GLY1324-LEU1344
C	VAL8-PRO28
C	ALA82-GLY102
C	MET118-TRP138
C	GLY161-LEU181
E	VAL1171-PRO1191
E	ALA1245-GLY1265
E	MET1281-TRP1301
E	GLY1324-LEU1344
G	VAL1171-PRO1191
G	ALA1245-GLY1265
G	MET1281-TRP1301
G	GLY1324-LEU1344

site_id	SWS_FT_FI7
Number of Residues	292
Details	TOPO_DOM: Extracellular => ECO:0000255

Chain	Residue	Details
A	MET1192-ARG1244
A	THR1302-MET1323
C	MET29-ARG81
C	THR139-MET160
E	MET1192-ARG1244
E	THR1302-MET1323
G	MET1192-ARG1244
G	THR1302-MET1323

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1011	proton shuttle (general acid/base)
A	ASP1020	covalent catalysis

site_id	MCSA2
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
C	GLU1011	proton shuttle (general acid/base)
C	ASP1020	covalent catalysis

site_id	MCSA3
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
E	GLU1011	proton shuttle (general acid/base)
E	ASP1020	covalent catalysis

site_id	MCSA4
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
G	GLU1011	proton shuttle (general acid/base)
G	ASP1020	covalent catalysis

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