Native human PPP1R15B-P-eIF2-eIF2B complex. Determined by electron microscopy at 3.8 Å resolution. Released 19 Nov 2025.
Explore 9HVF in 3D Show helices and sheets RCSB PDB PDBe
9HVF contains 34 α-helices and 59 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 | 189-199 | 11 | 18 |
| α-helix | 205-215 | 11 | |
| α-helix | 216-218 | 3 | |
| β-strand | 225-231 | 7 | 18 |
| β-strand | 234-241 | 8 | 18 |
| α-helix | 244-263 | 20 | |
| β-strand | 267-277 | 11 | 18 |
| α-helix | 280-297 | 18 | |
| α-helix | 299 | 1 | |
| β-strand | 300-301 | 2 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-22 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9 | 1 | 11 |
| α-helix | 16-18 | 3 | |
| α-helix | 33-36 | 4 | |
| β-strand | 42-47 | 6 | 12 |
| α-helix | 54-61 | 8 | |
| β-strand | 67-68 | 2 | 13 |
| β-strand | 82-88 | 7 | 12 |
| α-helix | 90-92 | 3 | |
| β-strand | 105 | 1 | 12 |
| β-strand | 113-114 | 2 | 14 |
| α-helix | 115 | 1 | |
| β-strand | 123-124 | 2 | 14 |
| β-strand | 128-134 | 7 | 12 |
| α-helix | 138-146 | 9 | |
| β-strand | 154-157 | 4 | 12 |
| α-helix | 168-180 | 13 | |
| β-strand | 185-190 | 6 | 12 |
| α-helix | 197-211 | 15 | |
| β-strand | 221-224 | 4 | 12 |
| α-helix | 233-241 | 9 | |
| β-strand | 255-262 | 8 | 15 |
| α-helix | 271-273 | 3 | |
| β-strand | 278-285 | 8 | 15 |
| β-strand | 295 | 1 | 15 |
| β-strand | 315 | 1 | 15 |
| β-strand | 318-322 | 5 | 15 |
| β-strand | 323 | 1 | 16 |
| β-strand | 326 | 1 | 16 |
| β-strand | 328 | 1 | 11 |
| β-strand | 337-341 | 5 | 15 |
| α-helix | 345-348 | 4 | |
| β-strand | 358-359 | 2 | 15 |
| β-strand | 370-377 | 8 | 17 |
| α-helix | 396-399 | 4 | |
| β-strand | 403-407 | 5 | 17 |
| β-strand | 412-420 | 9 | 17 |
| β-strand | 424-428 | 5 | 17 |
| β-strand | 440-447 | 8 | 17 |
| β-strand | 450-463 | 14 | 17 |
| α-helix | 464-466 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 1 |
| α-helix | 16-18 | 3 | |
| α-helix | 30-32 | 3 | |
| α-helix | 37-46 | 10 | |
| β-strand | 51 | 1 | 2 |
| β-strand | 52-55 | 4 | 1 |
| α-helix | 57-62 | 6 | |
| β-strand | 73 | 1 | 2 |
| β-strand | 76-77 | 2 | 1 |
| α-helix | 86-92 | 7 | |
| β-strand | 101-104 | 4 | 1 |
| β-strand | 108-110 | 3 | 3 |
| α-helix | 115-124 | 10 | |
| β-strand | 129-132 | 4 | 4 |
| β-strand | 133-134 | 2 | 5 |
| α-helix | 135-136 | 2 | |
| β-strand | 157-160 | 4 | 6 |
| β-strand | 166 | 1 | 7 |
| β-strand | 167-171 | 5 | 6 |
| α-helix | 185-188 | 4 | |
| β-strand | 196-197 | 2 | 6 |
| β-strand | 199-200 | 2 | 5 |
| β-strand | 205-206 | 2 | 4 |
| α-helix | 209-217 | 9 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-235 | 7 | |
| α-helix | 240-243 | 4 | |
| α-helix | 263-265 | 3 | |
| β-strand | 301 | 1 | 7 |
| β-strand | 302-304 | 3 | 4 |
| β-strand | 310-312 | 3 | 3 |
| α-helix | 317-325 | 9 | |
| α-helix | 328-333 | 6 | |
| β-strand | 345 | 1 | 8 |
| β-strand | 362-363 | 2 | 8 |
| β-strand | 374 | 1 | 9 |
| β-strand | 379-380 | 2 | 8 |
| β-strand | 391 | 1 | 9 |
| β-strand | 397 | 1 | 8 |
| β-strand | 403 | 1 | 10 |
| β-strand | 414 | 1 | 8 |
| β-strand | 420 | 1 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Translation initiation factor eIF-2B subunit gamma | E | protein | 452 | Homo sapiens | Q9NR50 (AlphaFold model) |
| Protein phosphatase 1 regulatory subunit 15B | A | protein | 109 | Homo sapiens | Q5SWA1 (AlphaFold model) |
| Eukaryotic translation initiation factor 2 subunit 2 | C | protein | 333 | Homo sapiens | P20042 (AlphaFold model) |
| Eukaryotic translation initiation factor 2 subunit 3 | D | protein | 472 | Homo sapiens | P41091 (AlphaFold model) |
| Eukaryotic translation initiation factor 2 subunit 1 | B | protein | 315 | Homo sapiens | P05198 |
>9HVF_1 Translation initiation factor eIF-2B subunit gamma (chains E) MEFQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQ KALCAEFKMKMKPDIVCIPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDL FRAYDASLAMLMRKGQDSIEPVPGQKGKKKAVEQRDFIGVDSTGKRLLFMANEADLDEEL VIKGSILQKHPRIRFHTGLVDAHLYCLKKYIVDFLMENGSITSIRSELIPYLVRKQFSSA SSQQGQEEKEEDLKKKELKSLDIYSFIKEANTLNLAPYDACWNACRGDRWEDLSRSQVRC YVHIMKEGLCSRVSTLGLYMEANRQVPKLLSALCPEEPPVHSSAQIVSKHLVGVDSLIGP ETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGAD IKDCLIGSGQRIEAKAKRVNEVIVGNDQLMEI
>9HVF_2 Protein phosphatase 1 regulatory subunit 15B (chains A) DYKDDDDKGDLPISARPACSNKLIDYILGGASSDLETSSDPEGEDWDEEAEDDGFDSDSS LSDSDLEQDPEGLHLWNSFCSVDPYNPQNFTATIQTAARIVPEEPSDSE
>9HVF_3 Eukaryotic translation initiation factor 2 subunit 2 (chains C) MSGDEMIFDPTMSKKKKKKKKPFMLDEEGDTQTEETQPSETKEVEPEPTEDKDLEADEED TRKKDASDDLDDLNFFNQKKKKKKTKKIFDIDEAEEGVKDLKIESDVQEPTEPEDDLDIM LGNKKKKKKNVKFPDEDEILEKDEALEDEDNKKDDGISFSNQTGPAWAGSERDYTYEELL NRVFNIMREKNPDMVAGEKRKFVMKPPQVVRVGTKKTSFVNFTDICKLLHRQPKHLLAFL LAELGTSGSIDGNNQLVIKGRFQQKQIENVLRRYIKEYVTCHTCRSPDTILQKDTRLYFL QCETCHSRCSVASIKTGFQAVTGKRAQLRAKAN
>9HVF_4 Eukaryotic translation initiation factor 2 subunit 3 (chains D) MAGGEAGVTLGQPHLSRQDLTTLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKA ISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGT KGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIM KLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIV KKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGI VSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGA VGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAV KADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD
>9HVF_5 Eukaryotic translation initiation factor 2 subunit 1 (chains B) MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSIN KLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLE YTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNI NRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTT TLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEV DGDDDAEEMEAKAED
Termination of the integrated stress response. De Miguel, C., Thorkelsson, S.R., Fatalska, A. et al. Science (2026) 391:eadw5137-eadw5137. DOI 10.1126/science.adw5137 · PubMed
Other PDB entries of the same protein (UniProt Q9NR50 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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