6H78: E1 enzyme for ubiquitin like protein activation
E1 enzyme for ubiquitin like protein activation. Determined by X-ray diffraction at 2.7 Å resolution. Released 31 Oct 2018.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organism
- Homo sapiens
- Chains
- 16
- Atoms
- 36,069
- Mol. weight
- 545.13 kDa
- Ligands
- ZN, MG, ATP
- Released
- 31 Oct 2018
Explore 6H78 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6H78 contains 227 α-helices and 227 β-strands across 16 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.
Chain A: 13 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 54-57 | 4 | |
| α-helix | 68-73 | 6 | |
| β-strand | 75-79 | 5 | 1 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-103 | 5 | 1 |
| β-strand | 107 | 1 | 2 |
| α-helix | 110-112 | 3 | |
| 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 | |
| α-helix | 174-175 | 2 | |
| β-strand | 177-180 | 4 | 1 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 1 |
| β-strand | 213-219 | 7 | 1 |
| β-strand | 221 | 1 | 3 |
| β-strand | 224 | 1 | 3 |
| α-helix | 232-235 | 4 | |
| α-helix | 255-274 | 20 | |
| β-strand | 282-286 | 5 | 1 |
| β-strand | 291 | 1 | 1 |
| β-strand | 294 | 1 | 1 |
| α-helix | 298-300 | 3 | |
| α-helix | 306-320 | 15 | |
Chain B: 15 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 54-61 | 8 | |
| α-helix | 68-73 | 6 | |
| β-strand | 75-79 | 5 | 4 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-103 | 5 | 4 |
| α-helix | 106 | 1 | |
| β-strand | 107 | 1 | 5 |
| α-helix | 108 | 1 | |
| α-helix | 110-112 | 3 | |
| α-helix | 120-122 | 3 | |
| β-strand | 126 | 1 | 5 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-147 | 5 | 4 |
| α-helix | 154-166 | 13 | |
| β-strand | 171 | 1 | 6 |
| β-strand | 173 | 1 | 6 |
| α-helix | 174-175 | 2 | |
| β-strand | 177-180 | 4 | 4 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 4 |
| β-strand | 213-219 | 7 | 4 |
| β-strand | 221 | 1 | 7 |
| β-strand | 224 | 1 | 7 |
| α-helix | 232 | 1 | |
| β-strand | 233-234 | 2 | 8 |
| α-helix | 255-274 | 20 | |
| β-strand | 282-286 | 5 | 4 |
| β-strand | 291 | 1 | 4 |
| β-strand | 294 | 1 | 4 |
| α-helix | 297-300 | 4 | |
| α-helix | 306-319 | 14 | |
Chain C: 15 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 57-62 | 6 | |
| α-helix | 68-73 | 6 | |
| β-strand | 75-79 | 5 | 9 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-103 | 5 | 9 |
| α-helix | 106 | 1 | |
| β-strand | 107 | 1 | 10 |
| α-helix | 108 | 1 | |
| α-helix | 110-114 | 5 | |
| α-helix | 120-122 | 3 | |
| β-strand | 126 | 1 | 10 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-147 | 5 | 9 |
| α-helix | 154-166 | 13 | |
| α-helix | 174-175 | 2 | |
| β-strand | 177-180 | 4 | 9 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 9 |
| β-strand | 213-219 | 7 | 9 |
| β-strand | 221 | 1 | 11 |
| β-strand | 224 | 1 | 11 |
| α-helix | 232-233 | 2 | |
| α-helix | 241-247 | 7 | |
| α-helix | 255-274 | 20 | |
| β-strand | 282-286 | 5 | 9 |
| β-strand | 291 | 1 | 9 |
| β-strand | 294 | 1 | 9 |
| α-helix | 306-320 | 15 | |
Chain D: 14 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 54-57 | 4 | |
| α-helix | 58-61 | 4 | |
| α-helix | 68-73 | 6 | |
| β-strand | 75-79 | 5 | 12 |
| α-helix | 83-94 | 12 | |
| β-strand | 99-103 | 5 | 12 |
| α-helix | 106 | 1 | |
| β-strand | 107 | 1 | 13 |
| α-helix | 108 | 1 | |
| α-helix | 110-112 | 3 | |
| α-helix | 120-122 | 3 | |
| β-strand | 126 | 1 | 13 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-147 | 5 | 12 |
| α-helix | 154-166 | 13 | |
| α-helix | 174-175 | 2 | |
| β-strand | 177-180 | 4 | 12 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 12 |
| β-strand | 213-219 | 7 | 12 |
| β-strand | 221 | 1 | 14 |
| β-strand | 224 | 1 | 14 |
| α-helix | 255-274 | 20 | |
| β-strand | 282-286 | 5 | 12 |
| β-strand | 291 | 1 | 12 |
| β-strand | 294 | 1 | 12 |
| α-helix | 306-320 | 15 | |
Chain E: 14 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 54-61 | 8 | |
| α-helix | 68-73 | 6 | |
| β-strand | 75-79 | 5 | 15 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-103 | 5 | 15 |
| β-strand | 107 | 1 | 16 |
| α-helix | 110-114 | 5 | |
| α-helix | 120-122 | 3 | |
| β-strand | 126 | 1 | 16 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-147 | 5 | 15 |
| α-helix | 154-166 | 13 | |
| α-helix | 174-175 | 2 | |
| β-strand | 177-180 | 4 | 15 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 15 |
| β-strand | 213-219 | 7 | 15 |
| β-strand | 221 | 1 | 17 |
| β-strand | 224 | 1 | 17 |
| α-helix | 232-233 | 2 | |
| α-helix | 241-247 | 7 | |
| α-helix | 255-274 | 20 | |
| β-strand | 282-286 | 5 | 15 |
| β-strand | 291 | 1 | 15 |
| β-strand | 294 | 1 | 15 |
| α-helix | 298-300 | 3 | |
| α-helix | 306-320 | 15 | |
Chain F: 15 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 54-57 | 4 | |
| α-helix | 58-62 | 5 | |
| α-helix | 68-73 | 6 | |
| β-strand | 75-79 | 5 | 18 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-103 | 5 | 18 |
| α-helix | 106 | 1 | |
| β-strand | 107 | 1 | 19 |
| α-helix | 108 | 1 | |
| α-helix | 110-114 | 5 | |
| α-helix | 120-122 | 3 | |
| β-strand | 123 | 1 | 20 |
| β-strand | 125 | 1 | 20 |
| β-strand | 126 | 1 | 19 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-147 | 5 | 18 |
| α-helix | 154-166 | 13 | |
| α-helix | 174-175 | 2 | |
| β-strand | 177-180 | 4 | 18 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 18 |
| β-strand | 213-219 | 7 | 18 |
| β-strand | 221 | 1 | 21 |
| β-strand | 224 | 1 | 21 |
| α-helix | 255-274 | 20 | |
| β-strand | 282-286 | 5 | 18 |
| β-strand | 291 | 1 | 18 |
| β-strand | 294 | 1 | 18 |
| α-helix | 298-300 | 3 | |
| α-helix | 306-319 | 14 | |
Chain G: 13 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 54-61 | 8 | |
| α-helix | 68-73 | 6 | |
| β-strand | 75-79 | 5 | 22 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-103 | 5 | 22 |
| β-strand | 107 | 1 | 23 |
| α-helix | 110-112 | 3 | |
| α-helix | 120-122 | 3 | |
| β-strand | 123 | 1 | 24 |
| β-strand | 125 | 1 | 24 |
| β-strand | 126 | 1 | 23 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-147 | 5 | 22 |
| α-helix | 154-166 | 13 | |
| α-helix | 174-175 | 2 | |
| β-strand | 177-180 | 4 | 22 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 22 |
| β-strand | 213-219 | 7 | 22 |
| β-strand | 221 | 1 | 25 |
| β-strand | 224 | 1 | 25 |
| α-helix | 232-233 | 2 | |
| α-helix | 255-274 | 20 | |
| β-strand | 282-286 | 5 | 22 |
| β-strand | 291 | 1 | 22 |
| β-strand | 294-295 | 2 | 22 |
| α-helix | 297-300 | 4 | |
| α-helix | 306-320 | 15 | |
Chain H: 15 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 54-57 | 4 | |
| α-helix | 68-73 | 6 | |
| β-strand | 75-79 | 5 | 26 |
| α-helix | 83-95 | 13 | |
| β-strand | 99-103 | 5 | 26 |
| α-helix | 106 | 1 | |
| β-strand | 107 | 1 | 27 |
| α-helix | 108 | 1 | |
| α-helix | 110-112 | 3 | |
| α-helix | 120-122 | 3 | |
| β-strand | 126 | 1 | 27 |
| α-helix | 127-138 | 12 | |
| β-strand | 143-147 | 5 | 26 |
| α-helix | 154-166 | 13 | |
| α-helix | 174-175 | 2 | |
| β-strand | 177-180 | 4 | 26 |
| α-helix | 185-198 | 14 | |
| β-strand | 202-207 | 6 | 26 |
| β-strand | 213-219 | 7 | 26 |
| β-strand | 221 | 1 | 28 |
| β-strand | 224 | 1 | 28 |
| α-helix | 232-235 | 4 | |
| α-helix | 255-274 | 20 | |
| β-strand | 282-286 | 5 | 26 |
| β-strand | 291 | 1 | 26 |
| β-strand | 294 | 1 | 26 |
| α-helix | 298-300 | 3 | |
| α-helix | 306-318 | 13 | |
8 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Ubiquitin-like modifier-activating enzyme 5 | A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | protein | 300 | Homo sapiens | Q9GZZ9 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P), FASTA
>6H78_1 Ubiquitin-like modifier-activating enzyme 5 (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P)
GRVRIEKMSSEVVDSNPYSRLMALKRMGIVSDYEKIRTFAVAIVGVGGVGSVTAEMLTRC
GIGKLLLFDYDKVELANMNRLFFQPHQAGLSKVQAAEHTLRNINPDVLFEVHNYNITTVE
NFQHFMDRISNGGLEEGKPVDLVLSCVDNFEARMTINTACNELGQTWMESGVSENAVSGH
IQLIIPGESACFACAPPLVVAANIDEKTLKREGVCAASLPTTMGVVAGILVQNVLKFLLN
FGTVSFYLGYNAMQDFFPTMSMKPNPQCDDRNCRKQQEEYKKKVAALPKQEVIQEEEEII
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 16 |
| MG | Magnesium ion | Mg | 32 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 16 |
Water and common crystallization additives (CL, EDO) are not listed.
Primary citation
An N-Terminal Extension to UBA5 Adenylation Domain Boosts UFM1 Activation: Isoform-Specific Differences in Ubiquitin-like Protein Activation. Soudah, N., Padala, P., Hassouna, F. et al. J Mol Biol (2019) 431:463-478. DOI 10.1016/j.jmb.2018.10.007 · PubMed
Other PDB entries of the same protein (UniProt Q9GZZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5IAA 1.85 Å, Crystal structure of human UBA5 in complex with UFM1
- 7NW1 1.95 Å, Crystal structure of UFC1 in complex with UBA5
- 3H8V 2.0 Å, Human Ubiquitin-activating Enzyme 5 in Complex with ATP
- 5IA8 2.0 Å, Structure of a Ubiquitin like protein with an E1 fragment
- 5L95 2.1 Å, Crystal structure of human UBA5 in complex with UFM1 and AMP
- 6H77 2.1 Å, E1 enzyme for ubiquitin like protein activation in complex with UBL
- 3GUC 2.25 Å, Human Ubiquitin-activating Enzyme 5 in Complex with AMPPNP
- 5HKH 2.55 Å, Crystal structure of Ufm1 in complex with UBA5
- 7NVK 2.65 Å, Crystal structure of UBA5 fragment fused to the N-terminus of UFC1
- 6H8C Structure of the human GABARAPL2 protein in complex with the UBA5 LIR motif
- 7OVC Structure of the human UFC1 protein in complex with the UBA5 C-terminal UFC1-binding…
Browse structure collections
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