1xtc Summary

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CHOLERA TOXIN

The structure was published by Zhang, R.G., Scott, D.L., Westbrook, M.L., et al., Spangler, B.D., Shipley, G.G., and Westbrook, E.M., in 1995 in a paper entitled "The three-dimensional crystal structure of cholera toxin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 1996.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 3 biomacromolecules, namely CHOLERA TOXIN.

The molecule most likely forms heteroheptamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A CHOLERA TOXIN P01555 (19-212) (CHTA_VIBCH)search Vibrio cholerae O1 biovar El Tor str. N16961search 100% 194 98%
C CHOLERA TOXIN P01555 (213-258) (CHTA_VIBCH)search Vibrio cholerae O1 biovar El Tor str. N16961search 100% 46 97%
D CHOLERA TOXIN P01556 (22-124) (CHTB_VIBCH)search Vibrio cholerae O1 biovar El Tor str. N16961search 99% 103 100%
E CHOLERA TOXIN P01556 (22-124) (CHTB_VIBCH)search Vibrio cholerae O1 biovar El Tor str. N16961search 99% 103 100%
F CHOLERA TOXIN P01556 (22-124) (CHTB_VIBCH)search Vibrio cholerae O1 biovar El Tor str. N16961search 99% 103 100%
G CHOLERA TOXIN P01556 (22-124) (CHTB_VIBCH)search Vibrio cholerae O1 biovar El Tor str. N16961search 99% 103 100%
H CHOLERA TOXIN P01556 (22-124) (CHTB_VIBCH)search Vibrio cholerae O1 biovar El Tor str. N16961search 99% 103 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P01555 (19 - 212) CHOLERA TOXIN Vibrio cholerae 569B
P01556 (22 - 124) CHOLERA TOXIN Vibrio cholerae 569B

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P01555) ADP-ribosylating toxinssearch Heat-Labile Enterotoxin, subunit Asearch PF01375: Heat-labile enterotoxin alpha chainsearch
C (P01555) ADP-ribosylating toxinssearch Single alpha-helices involved in coiled-coils or other helix-helix interfacessearch PF01375: Heat-labile enterotoxin alpha chainsearch
D, E, F, G, H (P01556) Bacterial AB5 toxins, B-subunitssearch OB fold (Dihydrolipoamide Acetyltransferase, E2P)search PF01376: Heat-labile enterotoxin beta chainsearch

Chain ID Cellular component (GO) Biological process (GO) Molecular function (GO)
A (P01555) extracellular regionsearch pathogenesissearch catalytic activitysearch
C (P01555) extracellular regionsearch pathogenesissearch catalytic activitysearch
D, E, F, G, H (P01556) host cell plasma membranesearch extracellular regionsearch membranesearch host cell membranesearch pathogenesissearch positive regulation of tyrosine phosphorylation of Stat3 proteinsearch protein ADP-ribosylationsearch killing of cells of other organismsearch host cell surface bindingsearch protein bindingsearch

Chain InterPro annotation
A Heat-labile enterotoxin, A chainsearch
C Heat-labile enterotoxin, A chainsearch
D, E, F, G, H Heat-labile enterotoxin, B chainsearch Enterotoxinsearch