A trichosanthin(tcs) MUTANT(E85R) complex structure with adenine. Determined by X-ray diffraction at 1.8 Å resolution. Released 3 Jun 2003.
Explore 1GIU in 3D Show helices and sheets RCSB PDB PDBe
1GIU contains 15 α-helices and 15 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 | 34-37 | 4 | 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 | 86-94 | 9 | |
| β-strand | 101-104 | 4 | 1 |
| α-helix | 111-118 | 8 | |
| α-helix | 122-124 | 3 | |
| β-strand | 127 | 1 | 3 |
| α-helix | 129-140 | 12 | |
| α-helix | 147-155 | 9 | |
| α-helix | 156-160 | 5 | |
| α-helix | 161-163 | 3 | |
| β-strand | 164 | 1 | 4 |
| α-helix | 165-172 | 8 | |
| β-strand | 179 | 1 | 3 |
| α-helix | 180-182 | 3 | |
| α-helix | 183-202 | 20 | |
| β-strand | 208-216 | 9 | 5 |
| β-strand | 222-227 | 6 | 5 |
| α-helix | 231-235 | 5 | |
| β-strand | 237 | 1 | 4 |
| β-strand | 240 | 1 | 2 |
| α-helix | 243-245 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ribosome-inactivating protein alpha-trichosanthin | A | protein | 247 | Trichosanthes kirilowii | P09989 (AlphaFold model) |
>1GIU_1 RIBOSOME-INACTIVATING PROTEIN ALPHA-TRICHOSANTHIN (chains A) DVSFRLSGATSSSYGVFISNLRKALPNERKLYDIPLLRSSLPGSQRYALIHLTNYADETI SVAIDVTNVYIMGYRAGDTSYFFNRASATEAAKYVFKDAMRKVTLPYSGNYERLQTAAGK IRENIPLGLPALDSAITTLFYYNANSAASALMVLIQSTSEAARYKFIEQQIGKRVDKTFL PSLAIISLENSWSALSKQIQIASTNNGQFESPVVLINAQNQRVTITNVDAGVVTSNIALL LNRNNMA
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADE | Adenine | C5 H5 N5 | 1 |
Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants. Guo, Q., Zhou, W., Too, H.M. et al. Protein Eng (2003) 16:391-396. DOI 10.1093/protein/gzg056 · 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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