Complex of [E160A-E189A] trichosanthin and adenine. Determined by X-ray diffraction at 1.93 Å resolution. Released 21 Jan 2003.
Explore 1NLI in 3D Show helices and sheets RCSB PDB PDBe
1NLI contains 15 α-helices and 17 β-strands across 1 chain. 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 1 |
| α-helix | 11-23 | 13 | |
| β-strand | 27-31 | 5 | 2 |
| β-strand | 34-35 | 2 | 2 |
| β-strand | 36 | 1 | 3 |
| β-strand | 37 | 1 | 2 |
| α-helix | 38 | 1 | |
| α-helix | 43-46 | 4 | |
| β-strand | 47-53 | 7 | 1 |
| β-strand | 59-65 | 7 | 1 |
| β-strand | 70-76 | 7 | 1 |
| β-strand | 79-82 | 4 | 1 |
| α-helix | 86-91 | 6 | |
| β-strand | 101-104 | 4 | 1 |
| α-helix | 111-118 | 8 | |
| α-helix | 122-124 | 3 | |
| β-strand | 127 | 1 | 4 |
| α-helix | 129-140 | 12 | |
| α-helix | 144-155 | 12 | |
| α-helix | 156-160 | 5 | |
| α-helix | 161-163 | 3 | |
| β-strand | 164 | 1 | 5 |
| α-helix | 165-173 | 9 | |
| β-strand | 179 | 1 | 4 |
| α-helix | 180-182 | 3 | |
| α-helix | 183-190 | 8 | |
| α-helix | 192-203 | 12 | |
| β-strand | 208-216 | 9 | 6 |
| β-strand | 222-227 | 6 | 6 |
| α-helix | 231-234 | 4 | |
| β-strand | 237 | 1 | 5 |
| β-strand | 240 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribosome-inactivating protein alpha-trichosanthin | A | protein | 248 | Trichosanthes kirilowii | P09989 (AlphaFold model) |
>1NLI_1 Ribosome-inactivating protein alpha-trichosanthin (chains A) MDVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYALIHLTNYADET ISVAIDVTNVYIMGYRAGDTSYFFNEASATEAAKYVFKDAMRKVTLPYSGNYERLQTAAG KIRENIPLGLPALDSAITTLFYYNANSAASALMVLIQSTSAAARYKFIEQQIGKRVDKTF LPSLAIISLANSWSALSKQIQIASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIAL LLNRNNMA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADE | Adenine | C5 H5 N5 | 1 |
Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine. Shaw, P.C., Wong, K.B., Chan, D.S. et al. Toxicon (2003) 41:575-581. DOI 10.1016/S0041-0101(02)00387-2 · PubMed
Other PDB entries of the same protein (UniProt P09989 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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