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

ElementResiduesLengthSheet
β-strand3-646
β-strand10-1237
β-strand18-2586
α-helix29-313
β-strand33-4087
β-strand44-5187
β-strand57-5937
α-helix61-633
β-strand67-7266
β-strand77-8266
α-helix84-863
β-strand88-9587
β-strand100C-10347
β-strand107-11157
α-helix115-1162
β-strand11718
β-strand120-12459
β-strand135-145119
β-strand14618
β-strand151-154410
α-helix155-1573
β-strand163-16539
α-helix166-1683
β-strand169-17139
β-strand174-184119
β-strand194-199610
α-helix200-2023
β-strand204-209610
Chain L: 7 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand4-741
β-strand10-1452
β-strand19-2571
β-strand33-3862
β-strand45-4952
β-strand53-5422
β-strand62-6761
β-strand70-7561
α-helix80-823
β-strand84-9072
α-helix961
β-strand97-9822
β-strand102-10762
β-strand11113
α-helix112-1132
β-strand114-11854
α-helix122-1265
β-strand130-139104
β-strand14013
β-strand145-15065
β-strand153-15535
β-strand159-16354
α-helix164-1674
β-strand173-18194
α-helix184-1874
β-strand191-19775
α-helix2041
β-strand205-21065

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
IgG1 TE33 FAB (light chain)Lprotein216Mus musculus
IgG1 TE33 FAB (heavy chain)Hprotein210Mus musculus
Cholera toxin peptide 3 (CTP3)Pprotein15P32890 (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

IDNameFormulaCopies
CITCitric acidC6 H8 O71

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:

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