Siah1 bound to synthetic peptide (ACE)KLRPV(ABA)MVRPTVR. Determined by X-ray diffraction at 3.0 Å resolution. Released 14 Aug 2013.
Explore 4I7B in 3D Show helices and sheets RCSB PDB PDBe
4I7B contains 21 α-helices and 34 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 | 96-97 | 2 | 1 |
| α-helix | 98 | 1 | |
| α-helix | 101-103 | 3 | |
| β-strand | 108-109 | 2 | 1 |
| α-helix | 111-113 | 3 | |
| α-helix | 115-118 | 4 | |
| α-helix | 125 | 1 | |
| β-strand | 126-127 | 2 | 2 |
| α-helix | 128 | 1 | |
| β-strand | 138-139 | 2 | 2 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-159 | 3 | 3 |
| β-strand | 162-168 | 7 | 4 |
| β-strand | 176-184 | 9 | 3 |
| β-strand | 187-196 | 10 | 3 |
| β-strand | 204-212 | 9 | 3 |
| α-helix | 215-218 | 4 | |
| β-strand | 221-229 | 9 | 4 |
| β-strand | 232-238 | 7 | 4 |
| α-helix | 239-240 | 2 | |
| β-strand | 241-242 | 2 | 3 |
| α-helix | 248-252 | 5 | |
| β-strand | 257-260 | 4 | 3 |
| α-helix | 261-267 | 7 | |
| β-strand | 268 | 1 | 4 |
| β-strand | 272-281 | 10 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 117-120 | 4 | 4 |
| α-helix | 121-122 | 2 | |
| β-strand | 123 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 96-97 | 2 | 5 |
| α-helix | 98 | 1 | |
| α-helix | 101-103 | 3 | |
| β-strand | 108-109 | 2 | 5 |
| α-helix | 111-117 | 7 | |
| β-strand | 126-127 | 2 | 6 |
| β-strand | 138-139 | 2 | 6 |
| α-helix | 141-151 | 11 | |
| β-strand | 157-159 | 3 | 7 |
| β-strand | 162-168 | 7 | 4 |
| β-strand | 176-184 | 9 | 7 |
| β-strand | 187-196 | 10 | 7 |
| β-strand | 204-211 | 8 | 7 |
| α-helix | 215-218 | 4 | |
| β-strand | 221-229 | 9 | 4 |
| β-strand | 232-238 | 7 | 4 |
| α-helix | 239-240 | 2 | |
| β-strand | 241-242 | 2 | 7 |
| α-helix | 248-252 | 5 | |
| β-strand | 257-260 | 4 | 7 |
| α-helix | 261-267 | 7 | |
| β-strand | 269 | 1 | 4 |
| β-strand | 272-281 | 10 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase SIAH1 | A, C | protein | 196 | Homo sapiens | Q8IUQ4 (AlphaFold model) |
| Protein phyllopod | B, D | protein | 14 | Drosophila melanogaster | Q27934 (AlphaFold model) |
>4I7B_1 E3 ubiquitin-protein ligase SIAH1 (chains A, C) GSHVANSVLFPCKYASSGCEITLPHTEKADHEELCEFRPYSCPCPGASCKWQGSLDAVMP HLMHQHKSITTLQGEDIVFLATDINLPGAVDWVMMQSCFGFHFMLVLEKQEKYDGHQQFF AIVQLIGTRKQAENFAYRLELNGHRRRLTWEATPRSIHEGIATAIMNSDCLVFDTSIAQL FAENGNLGINVTISMC
>4I7B_2 Protein phyllopod (chains B, D) XKLRPVAMVRPTVR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Structure-based design of covalent siah inhibitors. Stebbins, J.L., Santelli, E., Feng, Y. et al. Chem Biol (2013) 20:973-982. DOI 10.1016/j.chembiol.2013.06.008 · PubMed
Other PDB entries of the same protein (UniProt Q8IUQ4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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