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 | 0003824 | molecular_function | catalytic 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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 0003824 | molecular_function | catalytic 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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 0003824 | molecular_function | catalytic 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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 0003824 | molecular_function | catalytic 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 | 0016787 | molecular_function | hydrolase activity |
| 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 | 260 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 292 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 26 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 102 |
| Details | Region: {"description":"Interaction with EPHA2","evidences":[{"source":"PubMed","id":"16236711","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Active 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Active 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
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 |






