Crystal structure of human UBA5 in complex with UFM1. Determined by X-ray diffraction at 1.85 Å resolution. Released 28 Sept 2016.
Explore 5IAA in 3D Show helices and sheets RCSB PDB PDBe
5IAA contains 28 α-helices and 48 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 |
|---|---|---|---|
| α-helix | 71-73 | 3 | |
| β-strand | 75-79 | 5 | 1 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-103 | 5 | 1 |
| α-helix | 106 | 1 | |
| β-strand | 107 | 1 | 2 |
| α-helix | 108 | 1 | |
| α-helix | 120-122 | 3 | |
| β-strand | 126 | 1 | 2 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-147 | 5 | 1 |
| α-helix | 154-166 | 13 | |
| β-strand | 167 | 1 | 3 |
| β-strand | 173 | 1 | 3 |
| β-strand | 177-180 | 4 | 1 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 1 |
| β-strand | 213-219 | 7 | 1 |
| α-helix | 233-236 | 4 | |
| α-helix | 254-274 | 21 | |
| β-strand | 282-286 | 5 | 1 |
| β-strand | 291 | 1 | 1 |
| β-strand | 294-295 | 2 | 1 |
| α-helix | 297 | 1 | |
| β-strand | 298 | 1 | 4 |
| α-helix | 299 | 1 | |
| α-helix | 306-320 | 15 | |
| β-strand | 344-345 | 2 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 71-73 | 3 | |
| β-strand | 75-79 | 5 | 6 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-104 | 6 | 6 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-148 | 6 | 6 |
| α-helix | 154-166 | 13 | |
| β-strand | 167 | 1 | 7 |
| β-strand | 173 | 1 | 7 |
| β-strand | 177-180 | 4 | 6 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 6 |
| β-strand | 213-219 | 7 | 6 |
| β-strand | 221 | 1 | 8 |
| β-strand | 224 | 1 | 8 |
| α-helix | 227-229 | 3 | |
| α-helix | 233-236 | 4 | |
| α-helix | 254-274 | 21 | |
| β-strand | 282-286 | 5 | 6 |
| β-strand | 291 | 1 | 6 |
| β-strand | 294-295 | 2 | 6 |
| α-helix | 297 | 1 | |
| β-strand | 298 | 1 | 9 |
| α-helix | 299 | 1 | |
| α-helix | 306-320 | 15 | |
| β-strand | 344-345 | 2 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-10 | 6 | 10 |
| β-strand | 18-22 | 5 | 10 |
| β-strand | 28 | 1 | 11 |
| α-helix | 29-39 | 11 | |
| β-strand | 47-51 | 5 | 10 |
| β-strand | 55 | 1 | 4 |
| β-strand | 56-57 | 2 | 10 |
| β-strand | 62 | 1 | 11 |
| α-helix | 63-70 | 8 | |
| β-strand | 73-78 | 6 | 10 |
| β-strand | 82 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like modifier-activating enzyme 5 | A, B | protein | 290 | Homo sapiens | Q9GZZ9 (AlphaFold model) |
| Ubiquitin-fold modifier 1 | C, D | protein | 83 | Homo sapiens | P61960 (AlphaFold model) |
>5IAA_1 Ubiquitin-like modifier-activating enzyme 5 (chains A, B) MALKRMGIVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRCGIGKLLLFDYDKVELANMNRL FFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVENFQHFMDRISNGGLEEGKPVD LVLSCVDNFEARMTINTACNELGQTWMESGVSENAVSGHIQLIIPGESACFACAPPLVVA ANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLNFGTVSFYLGYNAMQDFFPTMS MKPNPQCDDRNCRKQQEEYKKKVAALPKQEVIQEEEEIIHEDNEWGIELV
>5IAA_2 Ubiquitin-fold modifier 1 (chains C, D) MSKVSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPA QTAGNVFLKHGSELRIIPRDRVG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Trans-Binding Mechanism of Ubiquitin-like Protein Activation Revealed by a UBA5-UFM1 Complex. Oweis, W., Padala, P., Hassouna, F. et al. Cell Rep (2016) 16:3113-3120. DOI 10.1016/j.celrep.2016.08.067 · PubMed
Other PDB entries of the same protein (UniProt Q9GZZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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