1TET: Anticholera toxin peptide complex

Crystal structure of an anticholera toxin peptide complex at 2.3 Å. Determined by X-ray diffraction at 2.3 Å resolution. Released 31 Jan 1994.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Mus musculus
Chains: 3
Atoms: 3,541
Mol. weight: 48.5 kDa
Ligands: CIT
Released: 31 Jan 1994

Explore 1TET in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1TET contains 14 α-helices and 42 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain H: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	6
β-strand	10-12	3	7
β-strand	18-25	8	6
α-helix	29-31	3
β-strand	33-40	8	7
β-strand	44-51	8	7
β-strand	57-59	3	7
α-helix	61-63	3
β-strand	67-72	6	6
β-strand	77-82	6	6
α-helix	84-86	3
β-strand	88-95	8	7
β-strand	100C-103	4	7
β-strand	107-111	5	7
α-helix	115-116	2
β-strand	117	1	8
β-strand	120-124	5	9
β-strand	135-145	11	9
β-strand	146	1	8
β-strand	151-154	4	10
α-helix	155-157	3
β-strand	163-165	3	9
α-helix	166-168	3
β-strand	169-171	3	9
β-strand	174-184	11	9
β-strand	194-199	6	10
α-helix	200-202	3
β-strand	204-209	6	10

Chain L: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-14	5	2
β-strand	19-25	7	1
β-strand	33-38	6	2
β-strand	45-49	5	2
β-strand	53-54	2	2
β-strand	62-67	6	1
β-strand	70-75	6	1
α-helix	80-82	3
β-strand	84-90	7	2
α-helix	96	1
β-strand	97-98	2	2
β-strand	102-107	6	2
β-strand	111	1	3
α-helix	112-113	2
β-strand	114-118	5	4
α-helix	122-126	5
β-strand	130-139	10	4
β-strand	140	1	3
β-strand	145-150	6	5
β-strand	153-155	3	5
β-strand	159-163	5	4
α-helix	164-167	4
β-strand	173-181	9	4
α-helix	184-187	4
β-strand	191-197	7	5
α-helix	204	1
β-strand	205-210	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
IgG1 TE33 FAB (light chain)	L	protein	216	Mus musculus
IgG1 TE33 FAB (heavy chain)	H	protein	210	Mus musculus
Cholera toxin peptide 3 (CTP3)	P	protein	15		P32890 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>1TET_1 IGG1 TE33 FAB (LIGHT CHAIN) (chains L)
DVLMTQTPLSLPVSLGDQASISCKSSQSIVHSSGNTYFEWYLQKPGQSPKLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHIPFTFGSGTKLEIKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYEWHNSYTCEATHKTSTSPIVKSFNR

Sequence of entity 2 (H), FASTA

>1TET_2 IGG1 TE33 FAB (HEAVY CHAIN) (chains H)
QIQLVQSGPELKTPGETVRISCKASGYTFTTYGMSWVKQTPGKGFKWMGWINTYSGVPTY
ADDFKGRFAFSLETSASTAYLQINNLKNEDTATYFCARRSWYFDVWGTGTTVTVSSAKTT
PPSVYPLAPGSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTV
PSSPRPSETVTCNVAHPASSTKVDKKIVPR

Sequence of entity 3 (P), FASTA

>1TET_3 CHOLERA TOXIN PEPTIDE 3 (CTP3) (chains P)
VEVPGSQHIDSQKKA

Ligands and cofactors

ID	Name	Formula	Copies
CIT	Citric acid	C6 H8 O7	1

Primary citation

Crystal structure of an anticholera toxin peptide complex at 2.3 A. Shoham, M. J Mol Biol (1993) 232:1169-1175. DOI 10.1006/jmbi.1993.1469 · PubMed

Other PDB entries of the same protein (UniProt P32890 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1DJR 1.3 Å, Heat-labile enterotoxin B-pentamer complexed with M-carboxyphenyl-alpha-D-galactose
6IAL 1.45 Å, Porcine E.coli heat-labile enterotoxin B-pentamer in complex with Lacto-N-neohexaose
1EFI 1.6 Å, Heat-labile enterotoxin B-pentamer complexed with para-aminophenyl-alpha-D-galactopyranos…
5LZI 1.6 Å, Porcine heat-labile enterotoxin R13H in complex with inhibitor MM146
1LT5 1.7 Å, Heat-labile enterotoxin B-pentamer complexed with thiodigalactoside
1EEF 1.8 Å, Heat-labile enterotoxin B-pentamer complexed with bound ligand pepg
1FD7 1.8 Å, Heat-labile enterotoxin B-pentamer with bound ligand BMSC001
2XRS 1.81 Å, Crystal structures exploring the origins of the broader specificity of escherichia coli…
1LTS 1.95 Å, Refined structure of E. Coli heat labile enterotoxin, a close relative of cholera toxin
1PZI 1.99 Å, Heat-Labile Enterotoxin B-Pentamer Complexed With Nitrophenyl Galactoside 2a
1LT3 2.0 Å, Heat-labile enterotoxin double mutant N40C/G166C
1LT4 2.0 Å, Heat-labile enterotoxin mutant S63K

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