9NB9: Viral protein DP71L
Viral protein DP71L in complex with phosphorylated eIF2alpha (NTD) and protein phosphatase 1A (D64A), stabilized by G-actin/DNAseI. Determined by electron microscopy at 3.03 Å resolution. Released 9 Jul 2025.
- Method
- Electron microscopy
- Resolution
- 3.03 Å
- Organisms
- African swine fever virus, Homo sapiens, Oryctolagus cuniculus
- Chains
- 5
- Atoms
- 9,423
- Mol. weight
- 141.84 kDa
- Ligands
- ATP, CA, MN
- Released
- 9 Jul 2025
Explore 9NB9 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9NB9 contains 58 α-helices and 63 β-strands across 5 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: 9 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-14 | 2 | |
| β-strand | 18-27 | 10 | 16 |
| β-strand | 30-35 | 6 | 16 |
| α-helix | 36-38 | 3 | |
| β-strand | 41-46 | 6 | 16 |
| α-helix | 47 | 1 | |
| α-helix | 59-61 | 3 | |
| β-strand | 67-76 | 10 | 16 |
| β-strand | 81-85 | 5 | 16 |
| α-helix | 91-117 | 27 | |
| α-helix | 123-140 | 18 | |
| α-helix | 146-157 | 12 | |
| α-helix | 159-165 | 7 | |
| α-helix | 169-183 | 15 | |
Chain B: 2 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 17-18 | 2 | 1 |
| β-strand | 23-26 | 4 | 1 |
| α-helix | 27-28 | 2 | |
| β-strand | 33 | 1 | 2 |
| α-helix | 36-68 | 33 | |
Chain C: 13 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-17 | 9 | |
| α-helix | 32-48 | 17 | |
| β-strand | 52-55 | 4 | 3 |
| β-strand | 59-62 | 4 | 1 |
| β-strand | 64 | 1 | 4 |
| α-helix | 69-79 | 11 | |
| β-strand | 87-89 | 3 | 1 |
| β-strand | 97 | 1 | 2 |
| α-helix | 100-113 | 14 | |
| β-strand | 118-120 | 3 | 1 |
| α-helix | 128-134 | 7 | |
| α-helix | 136-143 | 8 | |
| α-helix | 146-156 | 11 | |
| β-strand | 162-165 | 4 | 3 |
| β-strand | 169-172 | 4 | 3 |
| α-helix | 184-187 | 4 | |
| α-helix | 200-206 | 7 | |
| β-strand | 208-209 | 2 | 5 |
| β-strand | 216-218 | 3 | 5 |
| β-strand | 225-227 | 3 | 5 |
| α-helix | 229-239 | 11 | |
| β-strand | 243-246 | 4 | 3 |
| β-strand | 255-258 | 4 | 3 |
| α-helix | 259-261 | 3 | |
| β-strand | 263-266 | 4 | 3 |
| β-strand | 267 | 1 | 4 |
| α-helix | 272-274 | 3 | |
| β-strand | 280-285 | 6 | 1 |
| β-strand | 290-297 | 8 | 1 |
| α-helix | 298-299 | 2 | |
Chain D: 23 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-14 | 5 | 6 |
| β-strand | 18-23 | 6 | 6 |
| β-strand | 31-34 | 4 | 6 |
| β-strand | 37-40 | 4 | 7 |
| β-strand | 44-46 | 3 | 8 |
| β-strand | 55-56 | 2 | 7 |
| α-helix | 57-61 | 5 | |
| α-helix | 64-66 | 3 | |
| β-strand | 67-70 | 4 | 7 |
| β-strand | 73-74 | 2 | 9 |
| β-strand | 77-78 | 2 | 9 |
| α-helix | 81-90 | 10 | |
| α-helix | 91-96 | 6 | |
| α-helix | 100-102 | 3 | |
| β-strand | 105-109 | 5 | 6 |
| α-helix | 115-127 | 13 | |
| β-strand | 133-138 | 6 | 6 |
| α-helix | 139-147 | 9 | |
| β-strand | 152-157 | 6 | 10 |
| β-strand | 162-168 | 7 | 10 |
| β-strand | 171-172 | 2 | 10 |
| β-strand | 178-180 | 3 | 10 |
| α-helix | 184-195 | 12 | |
| α-helix | 196-198 | 3 | |
| α-helix | 207-218 | 12 | |
| α-helix | 225-234 | 10 | |
| α-helix | 236-238 | 3 | |
| β-strand | 240-243 | 4 | 11 |
| β-strand | 249-252 | 4 | 11 |
| α-helix | 255-261 | 7 | |
| α-helix | 266-269 | 4 | |
| α-helix | 276-286 | 11 | |
| α-helix | 289-297 | 9 | |
| β-strand | 299-302 | 4 | 10 |
| α-helix | 304-307 | 4 | |
| α-helix | 311-322 | 12 | |
| β-strand | 331-332 | 2 | 10 |
| α-helix | 337-339 | 3 | |
| α-helix | 340-349 | 10 | |
| α-helix | 354-356 | 3 | |
| β-strand | 359-360 | 2 | 6 |
| α-helix | 361-367 | 7 | |
| α-helix | 369-374 | 6 | |
Chain E: 11 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 25-33 | 9 | 8 |
| α-helix | 41-51 | 11 | |
| β-strand | 56-62 | 7 | 8 |
| α-helix | 68-77 | 10 | |
| β-strand | 86-89 | 4 | 8 |
| α-helix | 90-92 | 3 | |
| β-strand | 93 | 1 | 12 |
| β-strand | 100 | 1 | 12 |
| β-strand | 101-106 | 6 | 8 |
| β-strand | 112-118 | 7 | 13 |
| β-strand | 136-141 | 6 | 13 |
| β-strand | 149-156 | 8 | 13 |
| α-helix | 159-161 | 3 | |
| α-helix | 162-180 | 19 | |
| β-strand | 185-190 | 6 | 13 |
| α-helix | 202-205 | 4 | |
| α-helix | 207-210 | 4 | |
| β-strand | 214-216 | 3 | 13 |
| β-strand | 225 | 1 | 14 |
| β-strand | 234-239 | 6 | 13 |
| α-helix | 241-246 | 6 | |
| β-strand | 247 | 1 | 15 |
| α-helix | 248 | 1 | |
| β-strand | 253-254 | 2 | 8 |
| α-helix | 257-261 | 5 | |
| α-helix | 265-271 | 7 | |
| β-strand | 274 | 1 | 14 |
| β-strand | 277-279 | 3 | 8 |
| β-strand | 281 | 1 | 15 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein DP71L | B | protein | 71 | African swine fever virus | P0C753 |
| Serine/threonine-protein phosphatase PP1-alpha catalytic subunit | C | protein | 330 | Homo sapiens | P62136 (AlphaFold model) |
| Actin, alpha skeletal muscle | D | protein | 377 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Deoxyribonuclease-1 | E | protein | 282 | Bos taurus | P00639 (AlphaFold model) |
| Eukaryotic translation initiation factor 2 subunit 1 | A | protein | 186 | Homo sapiens | P05198 |
Sequence of entity 1 (B), FASTA
>9NB9_1 Protein DP71L (chains B)
MGGRRRKKRTNDVKHVRFAAAVEVWEADDIERKGPWEQAAVDRFRFQRRIASVEELLSAV
LLRQKKLLEQQ
Sequence of entity 2 (C), FASTA
>9NB9_2 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains C)
MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLK
ICGAIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
KNKGKYGQFSGLNPGGRPITPPRNSAKAKK
Sequence of entity 3 (D), FASTA
>9NB9_3 Actin, alpha skeletal muscle (chains D)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF
Sequence of entity 4 (E), FASTA
>9NB9_4 Deoxyribonuclease-1 (chains E)
MRGTRLMGLLLALAGLLQLGLSLKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQ
EVRDSHLVAVGKLLDYLNQDDPNTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYD
DGCESCGNDSFSREPAVVKFSSHSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKW
HLNDVMLMGDFNADCSYVTSSQWSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAG
SLLQSSVVPGSAAPFDFQAAYGLSNEMALAISDHYPVEVTLT
Sequence of entity 5 (A), FASTA
>9NB9_5 Eukaryotic translation initiation factor 2 subunit 1 (chains A)
PGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINK
LIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEY
TKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNIN
RRLTPQ
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| CA | Calcium ion | Ca | 1 |
| MN | Manganese (II) ion | Mn | 1 |
Primary citation
Harnessing the Evolution of Proteostasis Networks to Reverse Cognitive Dysfunction. Reineke, L.C., Zhu, P.J., Dalwadi, U. et al. bioRxiv (2025). DOI 10.1101/2025.02.28.640897 · PubMed
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