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5B2G

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0005198molecular_functionstructural molecule activity
A0005923cellular_componentbicellular tight junction
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
B0005576cellular_componentextracellular region
C0003796molecular_functionlysozyme activity
C0003824molecular_functioncatalytic activity
C0005198molecular_functionstructural molecule activity
C0005923cellular_componentbicellular tight junction
C0009253biological_processpeptidoglycan catabolic process
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0016998biological_processcell wall macromolecule catabolic process
C0030430cellular_componenthost cell cytoplasm
C0031640biological_processkilling of cells of another organism
C0042742biological_processdefense response to bacterium
C0044659biological_processviral release from host cell by cytolysis
D0005576cellular_componentextracellular region
E0003796molecular_functionlysozyme activity
E0003824molecular_functioncatalytic activity
E0005198molecular_functionstructural molecule activity
E0005923cellular_componentbicellular tight junction
E0009253biological_processpeptidoglycan catabolic process
E0016020cellular_componentmembrane
E0016787molecular_functionhydrolase activity
E0016798molecular_functionhydrolase activity, acting on glycosyl bonds
E0016998biological_processcell wall macromolecule catabolic process
E0030430cellular_componenthost cell cytoplasm
E0031640biological_processkilling of cells of another organism
E0042742biological_processdefense response to bacterium
E0044659biological_processviral release from host cell by cytolysis
F0005576cellular_componentextracellular region
G0003796molecular_functionlysozyme activity
G0003824molecular_functioncatalytic activity
G0005198molecular_functionstructural molecule activity
G0005923cellular_componentbicellular tight junction
G0009253biological_processpeptidoglycan catabolic process
G0016020cellular_componentmembrane
G0016787molecular_functionhydrolase activity
G0016798molecular_functionhydrolase activity, acting on glycosyl bonds
G0016998biological_processcell wall macromolecule catabolic process
G0030430cellular_componenthost cell cytoplasm
G0031640biological_processkilling of cells of another organism
G0042742biological_processdefense response to bacterium
G0044659biological_processviral release from host cell by cytolysis
H0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS01346
Number of Residues16
DetailsCLAUDIN Claudin family signature. GLWmnCvvqstgqm.QC
ChainResidueDetails
AGLY1212-CYS1227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues260
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues292
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues26
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues102
DetailsRegion: {"description":"Interaction with EPHA2","evidences":[{"source":"PubMed","id":"16236711","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

site_idMCSA2
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
CGLU1011proton shuttle (general acid/base)
CASP1020covalent catalysis

site_idMCSA3
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
EGLU1011proton shuttle (general acid/base)
EASP1020covalent catalysis

site_idMCSA4
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
GGLU1011proton shuttle (general acid/base)
GASP1020covalent catalysis

238895

PDB entries from 2025-07-16

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