Crystal structure of the complex of trichosanthin with adenine, obtained from trichosanthin complexed with the dinucleotide apg. Determined by X-ray diffraction at 1.86 Å resolution. Released 24 Apr 2000.
Explore 1QD2 in 3D Show helices and sheets RCSB PDB PDBe
1QD2 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 | 11-24 | 14 | |
| 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 | 183-202 | 20 | |
| β-strand | 208-216 | 9 | 6 |
| β-strand | 222-227 | 6 | 6 |
| α-helix | 231-235 | 5 | |
| β-strand | 237 | 1 | 5 |
| β-strand | 240 | 1 | 3 |
| α-helix | 243-245 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trichosanthin | A | protein | 247 | Trichosanthes kirilowii | P09989 (AlphaFold model) |
>1QD2_1 TRICHOSANTHIN (chains A) DVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYALIHLTNYADETI SVAIDVTNVYIMGYRAGDTSYFFNEASATEAAKYVFKDAMRKVTLPYSGNYERLQTAAGK IRENIPLGLPALDSAITTLFYYNANSAASALMVLIQSTSEAARYKFIEQQIGKRVDKTFL PSLAIISLENSWSALSKQIQIASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIALL LNRNNMA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADE | Adenine | C5 H5 N5 | 1 |
Crystal structures of the complexes of trichosanthin with four substrate analogs and catalytic mechanism of RNA N-glycosidase. Gu, Y.J., Xia, Z.X. Proteins (2000) 39:37-46. DOI 10.1002/(SICI)1097-0134(20000401)39:1<37::AID-PROT4>3.3.CO;2-7 · 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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