rRNA N-glycosylase RTA. Determined by X-ray diffraction at 1.55 Å resolution. Released 2 Nov 2016.
Explore 5GU4 in 3D Show helices and sheets RCSB PDB PDBe
5GU4 contains 31 α-helices and 30 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 1 |
| α-helix | 18-32 | 15 | |
| β-strand | 38-39 | 2 | 2 |
| β-strand | 42-43 | 2 | 2 |
| β-strand | 44 | 1 | 3 |
| α-helix | 45-47 | 3 | |
| α-helix | 53-55 | 3 | |
| β-strand | 57-63 | 7 | 1 |
| β-strand | 69-75 | 7 | 1 |
| β-strand | 81-86 | 6 | 1 |
| β-strand | 89-92 | 4 | 1 |
| α-helix | 93-95 | 3 | |
| α-helix | 98-103 | 6 | |
| α-helix | 104-106 | 3 | |
| β-strand | 113-116 | 4 | 1 |
| α-helix | 123-130 | 8 | |
| α-helix | 134-136 | 3 | |
| β-strand | 139 | 1 | 4 |
| α-helix | 141-154 | 14 | |
| α-helix | 161-171 | 11 | |
| α-helix | 172-177 | 6 | |
| α-helix | 178-180 | 3 | |
| α-helix | 182-193 | 12 | |
| β-strand | 198 | 1 | 4 |
| α-helix | 202-219 | 18 | |
| β-strand | 222 | 1 | 5 |
| β-strand | 225-233 | 9 | 5 |
| β-strand | 239-244 | 6 | 5 |
| α-helix | 245-248 | 4 | |
| β-strand | 255 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-12 | 5 | 6 |
| α-helix | 18-32 | 15 | |
| β-strand | 38-39 | 2 | 7 |
| β-strand | 42-43 | 2 | 7 |
| β-strand | 44 | 1 | 8 |
| α-helix | 45-47 | 3 | |
| α-helix | 53-55 | 3 | |
| β-strand | 57-63 | 7 | 6 |
| β-strand | 69-75 | 7 | 6 |
| β-strand | 81-86 | 6 | 6 |
| β-strand | 89-92 | 4 | 6 |
| α-helix | 98-104 | 7 | |
| β-strand | 113-116 | 4 | 6 |
| α-helix | 123-130 | 8 | |
| α-helix | 134-136 | 3 | |
| β-strand | 139 | 1 | 9 |
| α-helix | 141-154 | 14 | |
| α-helix | 161-171 | 11 | |
| α-helix | 172-177 | 6 | |
| α-helix | 178-180 | 3 | |
| α-helix | 182-193 | 12 | |
| β-strand | 198 | 1 | 9 |
| α-helix | 199-201 | 3 | |
| α-helix | 202-219 | 18 | |
| β-strand | 222 | 1 | 10 |
| β-strand | 225-233 | 9 | 10 |
| β-strand | 239-244 | 6 | 10 |
| α-helix | 246-248 | 3 | |
| β-strand | 255 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-6 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ricin | A, B | protein | 301 | Ricinus communis | P02879 (AlphaFold model) |
| Gly-phe-gly-leu-phe-asp | C, D | protein | 9 | Homo sapiens | P05387 (AlphaFold model) |
>5GU4_1 Ricin (chains A, B) MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSIFPKQYPIINFTTAGATVQSYTNFIR AVRGRLTTGADVRHEIPVLPNRVGLPINQRFILVELSNHAELSVTLALDVTNAYVVGYRA GNSAYFFHPDNQEDAEAITHLFTDVQNRYTFAFGGNYDRLEQLAGNLRENIELGNGPLEE AISALYYYSTGGTQLPTLARSFIICIQMISEAARFQYIEGEMRTRIRYNRRSAPDPSVIT LENSWGRLSTAIQESNQGAFASPIQLQRRNGSKFSVYDVSILIPIIALMVYRCAPPPSSQ F
>5GU4_2 GLY-PHE-GLY-LEU-PHE-ASP (chains C, D) DDMGFGLFD
Crystal Structure of Ribosome-Inactivating Protein Ricin A Chain in Complex with the C-Terminal Peptide of the Ribosomal Stalk Protein P2. Shi, W.W., Tang, Y.S., Sze, S.Y. et al. Toxins (Basel) (2016) 8. DOI 10.3390/toxins8100296 · PubMed
Other PDB entries of the same protein (UniProt P02879 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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