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

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