Eukaryotic translation initiation factor 2B tetramer. Determined by electron microscopy at 3.1 Å resolution. Released 6 Dec 2023.
Explore 8TQO in 3D Show helices and sheets RCSB PDB PDBe
8TQO contains 57 α-helices and 102 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 | 44-48 | 5 | 1 |
| α-helix | 65-67 | 3 | |
| β-strand | 69 | 1 | 2 |
| β-strand | 74 | 1 | 2 |
| α-helix | 75-86 | 12 | |
| β-strand | 90-95 | 6 | 1 |
| α-helix | 99-107 | 9 | |
| β-strand | 119-124 | 6 | 1 |
| α-helix | 131-140 | 10 | |
| β-strand | 148-152 | 5 | 1 |
| β-strand | 155-157 | 3 | 3 |
| α-helix | 162-174 | 13 | |
| β-strand | 179-187 | 9 | 1 |
| β-strand | 201-206 | 6 | 1 |
| β-strand | 211-217 | 7 | 1 |
| β-strand | 223-225 | 3 | 4 |
| α-helix | 229-233 | 5 | |
| β-strand | 238-241 | 4 | 1 |
| β-strand | 244-252 | 9 | 1 |
| α-helix | 254-262 | 9 | |
| α-helix | 269-278 | 10 | |
| β-strand | 286-292 | 7 | 1 |
| β-strand | 297-299 | 3 | 3 |
| α-helix | 303-314 | 12 | |
| β-strand | 337-338 | 2 | 5 |
| β-strand | 342-344 | 3 | 5 |
| β-strand | 350 | 1 | 6 |
| α-helix | 351 | 1 | |
| β-strand | 355-356 | 2 | 7 |
| β-strand | 360-362 | 3 | 5 |
| β-strand | 367 | 1 | 8 |
| β-strand | 368 | 1 | 6 |
| β-strand | 373-375 | 3 | 7 |
| β-strand | 378-379 | 2 | 5 |
| β-strand | 384 | 1 | 8 |
| β-strand | 390-392 | 3 | 7 |
| β-strand | 395-396 | 2 | 5 |
| β-strand | 401-402 | 2 | 8 |
| β-strand | 407-409 | 3 | 7 |
| β-strand | 411-413 | 3 | 5 |
| β-strand | 418-419 | 2 | 8 |
| β-strand | 424-425 | 2 | 7 |
| β-strand | 429-431 | 3 | 5 |
| β-strand | 436 | 1 | 8 |
| β-strand | 442-443 | 2 | 7 |
| β-strand | 448-449 | 2 | 5 |
| β-strand | 457 | 1 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-24 | 16 | |
| α-helix | 31-47 | 17 | |
| α-helix | 54-71 | 18 | |
| α-helix | 77-97 | 21 | |
| α-helix | 129-145 | 17 | |
| α-helix | 149-152 | 4 | |
| α-helix | 155-158 | 4 | |
| β-strand | 164-168 | 5 | 17 |
| α-helix | 172-181 | 10 | |
| β-strand | 188-192 | 5 | 17 |
| α-helix | 193-194 | 2 | |
| α-helix | 200-208 | 9 | |
| β-strand | 214-217 | 4 | 17 |
| α-helix | 219-221 | 3 | |
| α-helix | 222-225 | 4 | |
| β-strand | 231-234 | 4 | 17 |
| β-strand | 239 | 1 | 18 |
| β-strand | 245 | 1 | 18 |
| β-strand | 248 | 1 | 19 |
| α-helix | 251-260 | 10 | |
| β-strand | 265-268 | 4 | 17 |
| α-helix | 271-273 | 3 | |
| β-strand | 274 | 1 | 18 |
| β-strand | 288 | 1 | 20 |
| α-helix | 297-299 | 3 | |
| α-helix | 301-303 | 3 | |
| β-strand | 306-308 | 3 | 21 |
| β-strand | 311 | 1 | 20 |
| β-strand | 313 | 1 | 19 |
| β-strand | 316 | 1 | 18 |
| α-helix | 318-320 | 3 | |
| β-strand | 323-325 | 3 | 17 |
| β-strand | 331 | 1 | 17 |
| α-helix | 338-343 | 6 | |
| α-helix | 346-348 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 168-171 | 4 | |
| α-helix | 175-177 | 3 | |
| β-strand | 185 | 1 | 22 |
| α-helix | 205-216 | 12 | |
| α-helix | 222-239 | 18 | |
| α-helix | 242-243 | 2 | |
| α-helix | 248-266 | 19 | |
| α-helix | 268-270 | 3 | |
| α-helix | 271-285 | 15 | |
| α-helix | 293-308 | 16 | |
| α-helix | 309-313 | 5 | |
| α-helix | 315-324 | 10 | |
| β-strand | 332-336 | 5 | 21 |
| α-helix | 340-350 | 11 | |
| β-strand | 357-362 | 6 | 21 |
| α-helix | 369-378 | 10 | |
| β-strand | 383-387 | 5 | 21 |
| α-helix | 388-390 | 3 | |
| α-helix | 391-394 | 4 | |
| α-helix | 395-397 | 3 | |
| β-strand | 400-404 | 5 | 21 |
| β-strand | 407-408 | 2 | 23 |
| β-strand | 414-417 | 4 | 23 |
| α-helix | 420-429 | 10 | |
| β-strand | 434-437 | 4 | 21 |
| α-helix | 440-442 | 3 | |
| β-strand | 443 | 1 | 23 |
| β-strand | 457 | 1 | 22 |
| α-helix | 460-462 | 3 | |
| β-strand | 482-484 | 3 | 17 |
| β-strand | 489-492 | 4 | 23 |
| β-strand | 499-501 | 3 | 21 |
| β-strand | 502 | 1 | 24 |
| β-strand | 505 | 1 | 24 |
| α-helix | 512-516 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-8 | 5 | 9 |
| α-helix | 25-27 | 3 | |
| β-strand | 29-30 | 2 | 10 |
| β-strand | 33-34 | 2 | 10 |
| α-helix | 37-43 | 7 | |
| β-strand | 51-53 | 3 | 9 |
| β-strand | 76-77 | 2 | 9 |
| α-helix | 86-92 | 7 | |
| β-strand | 101-105 | 5 | 9 |
| β-strand | 109 | 1 | 11 |
| α-helix | 115-123 | 9 | |
| β-strand | 128-133 | 6 | 9 |
| β-strand | 156-161 | 6 | 1 |
| β-strand | 166 | 1 | 9 |
| β-strand | 167-172 | 6 | 1 |
| β-strand | 181-183 | 3 | 4 |
| α-helix | 184-189 | 6 | |
| β-strand | 192-196 | 5 | 1 |
| β-strand | 200-207 | 8 | 9 |
| α-helix | 209-217 | 9 | |
| α-helix | 228-234 | 7 | |
| β-strand | 300-305 | 6 | 9 |
| β-strand | 311 | 1 | 11 |
| α-helix | 316-333 | 18 | |
| β-strand | 341 | 1 | 12 |
| β-strand | 353-354 | 2 | 13 |
| β-strand | 358 | 1 | 12 |
| β-strand | 369-371 | 3 | 13 |
| β-strand | 374 | 1 | 14 |
| β-strand | 375 | 1 | 12 |
| β-strand | 377 | 1 | 15 |
| β-strand | 386-388 | 3 | 13 |
| β-strand | 391-392 | 2 | 14 |
| β-strand | 394 | 1 | 15 |
| β-strand | 397 | 1 | 16 |
| β-strand | 403-405 | 3 | 13 |
| β-strand | 408-409 | 2 | 14 |
| β-strand | 414-415 | 2 | 16 |
| β-strand | 420-422 | 3 | 13 |
| β-strand | 425-426 | 2 | 14 |
| β-strand | 431-432 | 2 | 16 |
| β-strand | 436-437 | 2 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Translation initiation factor eIF-2B subunit epsilon | A | protein | 721 | Homo sapiens | Q13144 (AlphaFold model) |
| Translation initiation factor eIF-2B subunit gamma | I | protein | 452 | Homo sapiens | Q9NR50 (AlphaFold model) |
| Translation initiation factor eIF-2B subunit beta | D | protein | 368 | Homo sapiens | P49770 (AlphaFold model) |
| Translation initiation factor eIF-2B subunit delta | E | protein | 523 | Homo sapiens | Q9UI10 (AlphaFold model) |
>8TQO_1 Translation initiation factor eIF-2B subunit epsilon (chains A) MAAPVVAPPGVVVSRANKRSGAGPGGSGGGGARGAEEEPPPPLQAVLVADSFDRRFFPIS KDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVV RIITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVSV MTMIFKESSPSHPTRCHEDNVVVAVDSTTNRVLHFQKTQGLRRFAFPLSLFQGSSDGVEV RYDLLDCHISICSPQVAQLFTDNFDYQTRDDFVRGLLVNEEILGNQIHMHVTAKEYGARV SNLHMYSAVCADVIRRWVYPLTPEANFTDSTTQSCTHSRHNIYRGPEVSLGHGSILEENV LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVK ERVTLKPRSVLTSQVVVGPNITLPEGSVISLHPPDAEEDEDDGEFSDDSGADQEKDKVKM KGYNPAEVGAAGKGYLWKAAGMNMEEEEELQQNLWGLKINMEEESESESEQSMDSEEPDS RGGSPQMDDIKVFQNEVLGTLQRGKEENISCDNLVLEINSLKYAYNVSLKEVMQVLSHVV LEFPLQQMDSPLDSSRYCALLLPLLKAWSPVFRNYIKRAADHLEALAAIEDFFLEHEALG ISMAKVLMAFYQLEILAEETILSWFSQRDTTDKGQQLRKNQQLQRFIQWLKEAEEESSED D
>8TQO_2 Translation initiation factor eIF-2B subunit gamma (chains I) MEFQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQ KALCAEFKMKMKPDIVCIPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDL FRAYDASLAMLMRKGQDSIEPVPGQKGKKKAVEQRDFIGVDSTGKRLLFMANEADLDEEL VIKGSILQKHPRIRFHTGLVDAHLYCLKKYIVDFLMENGSITSIRSELIPYLVRKQFSSA SSQQGQEEKEEDLKKKELKSLDIYSFIKEANTLNLAPYDACWNACRGDRWEDLSRSQVRC YVHIMKEGLCSRVSTLGLYMEANRQVPKLLSALCPEEPPVHSSAQIVSKHLVGVDSLIGP ETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGAD IKDCLIGSGQRIEAKAKRVNEVIVGNDQLMEI
>8TQO_3 Translation initiation factor eIF-2B subunit beta (chains D) MHHHHHHGGGSENLYFQSPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLR QIITDHRWSNAGELMELIRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRSDES DQQESLHKLLTSGGLNEDFSFHYAQLQSNIIEAINELLVELEGTMENIAAQALEHIHSNE VIMTIGFSRTVEAFLKEAARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIF AVMSRVNKVIIGTKTILANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEED SFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSEL YHPDDHVL
>8TQO_4 Translation initiation factor eIF-2B subunit delta (chains E) MAAVAVAVREDSGSGMKAELPPGPGAVGREMTKEEKLQLRKEKKQQKKKRKEEKGAEPET GSAVSAAQCQVGPTRELPESGIQLGTPREKVPAGRSKAELRAERRAKQEAERALKQARKG EQGGPPPKASPSTAGETPSGVKRLPEYPQVDDLLLRRLVKKPERQQVPTRKDYGSKVSLF SHLPQYSRQNSLTQFMSIPSSVIHPAMVRLGLQYSQGLVSGSNARCIALLRALQQVIQDY TTPPNEELSRDLVNKLKPYMSFLTQCRPLSASMHNAIKFLNKEITSVGSSKREEEAKSEL RAAIDRYVQEKIVLAAQAISRFAYQKISNGDVILVYGCSSLVSRILQEAWTEGRRFRVVV VDSRPWLEGRHTLRSLVHAGVPASYLLIPAASYVLPEVSKVLLGAHALLANGSVMSRVGT AQLALVARAHNVPVLVCCETYKFCERVQTDAFVSNELDDPDDLQCKRGEHVALANWQNHA SLRLLNLVYDVTPPELVDLVITELGMIPCSSVPVVLRVKSSDQ
A helical fulcrum in eIF2B coordinates allosteric regulation of stress signaling. Lawrence, R.E., Shoemaker, S.R., Deal, A. et al. Nat Chem Biol (2024) 20:422-431. DOI 10.1038/s41589-023-01453-9 · PubMed
Other PDB entries of the same protein (UniProt Q13144 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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