Structure of a human 48S translational initiation complex - eIF2-TC. Determined by electron microscopy at 3.8 Å resolution. Released 16 Sept 2020.
Explore 6YBV in 3D Show helices and sheets RCSB PDB PDBe
6YBV contains 31 α-helices and 46 β-strands across 3 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 | 7 | 1 | 4 |
| α-helix | 14-15 | 2 | |
| β-strand | 19-24 | 6 | 5 |
| β-strand | 31-36 | 6 | 5 |
| β-strand | 39 | 1 | 4 |
| β-strand | 42-47 | 6 | 5 |
| α-helix | 59-62 | 4 | |
| β-strand | 68-75 | 8 | 5 |
| β-strand | 84-86 | 3 | 5 |
| α-helix | 92-118 | 27 | |
| α-helix | 124-130 | 7 | |
| α-helix | 131-136 | 6 | |
| α-helix | 137-141 | 5 | |
| α-helix | 147-156 | 10 | |
| α-helix | 162-165 | 4 | |
| α-helix | 170-180 | 11 | |
| β-strand | 191-195 | 5 | 6 |
| β-strand | 196-197 | 2 | 7 |
| α-helix | 204-217 | 14 | |
| β-strand | 226-229 | 4 | 6 |
| β-strand | 235-239 | 5 | 6 |
| α-helix | 244-261 | 18 | |
| β-strand | 269-270 | 2 | 7 |
| β-strand | 276 | 1 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 177-185 | 9 | |
| α-helix | 189 | 1 | |
| β-strand | 218-219 | 2 | 1 |
| α-helix | 222-228 | 7 | |
| α-helix | 235-242 | 8 | |
| α-helix | 243-245 | 3 | |
| β-strand | 248-249 | 2 | 1 |
| β-strand | 256-258 | 3 | 1 |
| α-helix | 264-274 | 11 | |
| α-helix | 275-279 | 5 | |
| β-strand | 281 | 1 | 2 |
| β-strand | 284 | 1 | 2 |
| β-strand | 291-293 | 3 | 3 |
| β-strand | 298-300 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 44-47 | 4 | 8 |
| α-helix | 54-62 | 9 | |
| α-helix | 70-75 | 6 | |
| α-helix | 81-82 | 2 | |
| β-strand | 84-86 | 3 | 8 |
| β-strand | 130-134 | 5 | 8 |
| α-helix | 142-151 | 10 | |
| β-strand | 154-159 | 6 | 8 |
| α-helix | 169-180 | 12 | |
| β-strand | 186-189 | 4 | 8 |
| α-helix | 197-211 | 15 | |
| α-helix | 215-218 | 4 | |
| β-strand | 221-223 | 3 | 8 |
| β-strand | 225 | 1 | 9 |
| β-strand | 230 | 1 | 9 |
| α-helix | 232-242 | 11 | |
| α-helix | 244-246 | 3 | |
| α-helix | 253-254 | 2 | |
| β-strand | 255-257 | 3 | 10 |
| β-strand | 279-281 | 3 | 11 |
| β-strand | 283-285 | 3 | 10 |
| β-strand | 293-296 | 4 | 10 |
| α-helix | 312-313 | 2 | |
| β-strand | 314-317 | 4 | 10 |
| β-strand | 321-323 | 3 | 11 |
| β-strand | 326 | 1 | 11 |
| β-strand | 337-339 | 3 | 11 |
| α-helix | 340 | 1 | |
| α-helix | 345-348 | 4 | |
| β-strand | 357-360 | 4 | 10 |
| β-strand | 367-368 | 2 | 12 |
| β-strand | 372-377 | 6 | 13 |
| β-strand | 403-408 | 6 | 13 |
| β-strand | 411-413 | 3 | 13 |
| β-strand | 415-420 | 6 | 13 |
| β-strand | 424-429 | 6 | 13 |
| β-strand | 433-434 | 2 | 12 |
| β-strand | 440-447 | 8 | 13 |
| β-strand | 450-459 | 10 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Eukaryotic translation initiation factor 2 subunit 2 | s | protein | 333 | Homo sapiens | P20042 (AlphaFold model) |
| Eukaryotic translation initiation factor 2 subunit 1 | r | protein | 315 | Homo sapiens | P05198 (AlphaFold model) |
| Initiator methionine tRNA | w | RNA | 75 | Homo sapiens | |
| mRNA | k | RNA | 3 | Homo sapiens | |
| Eukaryotic translation initiation factor 2 subunit 3 | t | protein | 472 | Homo sapiens | P41091 (AlphaFold model) |
>6YBV_1 Eukaryotic translation initiation factor 2 subunit 2 (chains s) MSGDEMIFDPTMSKKKKKKKKPFMLDEEGDTQTEETQPSETKEVEPEPTEDKDLEADEED TRKKDASDDLDDLNFFNQKKKKKKTKKIFDIDEAEEGVKDLKIESDVQEPTEPEDDLDIM LGNKKKKKKNVKFPDEDEILEKDEALEDEDNKKDDGISFSNQTGPAWAGSERDYTYEELL NRVFNIMREKNPDMVAGEKRKFVMKPPQVVRVGTKKTSFVNFTDICKLLHRQPKHLLAFL LAELGTSGSIDGNNQLVIKGRFQQKQIENVLRRYIKEYVTCHTCRSPDTILQKDTRLYFL QCETCHSRCSVASIKTGFQAVTGKRAQLRAKAN
>6YBV_2 Eukaryotic translation initiation factor 2 subunit 1 (chains r) MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSIN KLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLE YTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNI NRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTT TLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEV DGDDDAEEMEAKAED
>6YBV_3 Initiator methionine tRNA (chains w) AGCAGAGUGGCGCAGCGGAAGCGUGCUGGGCCCAUAACCCAGAGGUCGAUGGAUCGAAAC CAUCCUCUGCUACCA
>6YBV_4 mRNA (chains k) AAA
>6YBV_5 Eukaryotic translation initiation factor 2 subunit 3 (chains t) MAGGEAGVTLGQPHLSRQDLTTLDVTKLTPLSHEVISRQATINIGTIGHVAHGKSTVVKA ISGVHTVRFKNELERNITIKLGYANAKIYKLDDPSCPRPECYRSCGSSTPDEFPTDIPGT KGNFKLVRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAGNESCPQPQTSEHLAAIEIM KLKHILILQNKIDLVKESQAKEQYEQILAFVQGTVAEGAPIIPISAQLKYNIEVVCEYIV KKIPVPPRDFTSEPRLIVIRSFDVNKPGCEVDDLKGGVAGGSILKGVLKVGQEIEVRPGI VSKDSEGKLMCKPIFSKIVSLFAEHNDLQYAAPGGLIGVGTKIDPTLCRADRMVGQVLGA VGALPEIFTELEISYFLLRRLLGVRTEGDKKAAKVQKLSKNEVLMVNIGSLSTGGRVSAV KADLGKIVLTNPVCTEVGEKIALSRRVEKHWRLIGWGQIRRGVTIKPTVDDD
Structure of a human 48Stranslational initiation complex. Brito Querido, J., Sokabe, M., Kraatz, S. et al. Science (2020) 369:1220-1227. DOI 10.1126/science.aba4904 · PubMed
Other PDB entries of the same protein (UniProt P20042 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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