7LSX: Proteasome subunit alpha type-1
Cryo-EM structure of 13S proteasome core particle assembly intermediate purified from Pre3-1 proteasome mutant (G34D). Determined by electron microscopy at 3.61 Å resolution. Released 14 Apr 2021.
- Method
- Electron microscopy
- Resolution
- 3.61 Å
- Organism
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
- Chains
- 13
- Atoms
- 22,217
- Mol. weight
- 350.04 kDa
- Released
- 14 Apr 2021
Explore 7LSX in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7LSX contains 125 α-helices and 166 β-strands across 13 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: 10 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-14 | 3 | |
| α-helix | 26-34 | 9 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 50-56 | 7 | 1 |
| β-strand | 64 | 1 | 2 |
| α-helix | 66-68 | 3 | |
| β-strand | 72-74 | 3 | 3 |
| β-strand | 79-84 | 6 | 3 |
| α-helix | 87-108 | 22 | |
| α-helix | 111-113 | 3 | |
| α-helix | 114-130 | 17 | |
| β-strand | 131 | 1 | 4 |
| β-strand | 134 | 1 | 5 |
| β-strand | 140-147 | 8 | 3 |
| β-strand | 151-157 | 7 | 3 |
| β-strand | 163-166 | 4 | 3 |
| β-strand | 168-171 | 4 | 1 |
| α-helix | 175-189 | 15 | |
| α-helix | 199-214 | 16 | |
| α-helix | 220-222 | 3 | |
| β-strand | 223-229 | 7 | 1 |
| β-strand | 233-235 | 3 | 1 |
| α-helix | 238-250 | 13 | |
Chain B: 15 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 12 | 1 | 6 |
| β-strand | 18 | 1 | 6 |
| α-helix | 19-30 | 12 | |
| α-helix | 32-33 | 2 | |
| β-strand | 34-38 | 5 | 7 |
| β-strand | 43-48 | 6 | 7 |
| β-strand | 56 | 1 | 3 |
| α-helix | 58-60 | 3 | |
| β-strand | 65-68 | 4 | 8 |
| β-strand | 71-77 | 7 | 8 |
| α-helix | 79-92 | 14 | |
| α-helix | 93-98 | 6 | |
| α-helix | 99-101 | 3 | |
| α-helix | 104-106 | 3 | |
| α-helix | 107-122 | 16 | |
| β-strand | 127 | 1 | 4 |
| α-helix | 128-130 | 3 | |
| β-strand | 132-140 | 9 | 8 |
| β-strand | 144-150 | 7 | 8 |
| β-strand | 156-158 | 3 | 8 |
| β-strand | 159 | 1 | 9 |
| β-strand | 161-164 | 4 | 7 |
| α-helix | 168-178 | 11 | |
| α-helix | 185-199 | 15 | |
| β-strand | 209-214 | 6 | 7 |
| α-helix | 219-221 | 3 | |
| β-strand | 224-225 | 2 | 10 |
| α-helix | 231-233 | 3 | |
| β-strand | 235-237 | 3 | 7 |
| α-helix | 238-239 | 2 | |
| α-helix | 240-248 | 9 | |
Chain C: 10 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 20-29 | 10 | |
| α-helix | 33-34 | 2 | |
| β-strand | 35-39 | 5 | 11 |
| β-strand | 43-49 | 7 | 11 |
| β-strand | 57 | 1 | 9 |
| β-strand | 66-70 | 5 | 12 |
| β-strand | 73-79 | 7 | 12 |
| α-helix | 81-102 | 22 | |
| α-helix | 105-107 | 3 | |
| α-helix | 108-122 | 15 | |
| β-strand | 125 | 1 | 13 |
| α-helix | 129-131 | 3 | |
| β-strand | 133-139 | 7 | 12 |
| β-strand | 147-151 | 5 | 12 |
| β-strand | 157-160 | 4 | 12 |
| β-strand | 162-165 | 4 | 11 |
| α-helix | 169-179 | 11 | |
| α-helix | 186-200 | 15 | |
| α-helix | 208-210 | 3 | |
| β-strand | 211-217 | 7 | 11 |
| β-strand | 226-228 | 3 | 11 |
| α-helix | 232-241 | 10 | |
Chain D: 9 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 18-27 | 10 | |
| α-helix | 31-32 | 2 | |
| β-strand | 33-37 | 5 | 14 |
| β-strand | 42-47 | 6 | 14 |
| β-strand | 55 | 1 | 12 |
| β-strand | 65-68 | 4 | 15 |
| β-strand | 71-73 | 3 | 15 |
| β-strand | 77 | 1 | 16 |
| α-helix | 79-99 | 21 | |
| α-helix | 106-119 | 14 | |
| β-strand | 126 | 1 | 13 |
| α-helix | 127-129 | 3 | |
| β-strand | 131 | 1 | 16 |
| β-strand | 136-138 | 3 | 15 |
| β-strand | 145-147 | 3 | 15 |
| β-strand | 148-150 | 3 | 17 |
| β-strand | 156-158 | 3 | 17 |
| β-strand | 159 | 1 | 18 |
| β-strand | 161-164 | 4 | 14 |
| α-helix | 168-178 | 11 | |
| α-helix | 188-200 | 13 | |
| α-helix | 207-209 | 3 | |
| β-strand | 210-216 | 7 | 14 |
| β-strand | 220-223 | 4 | 14 |
| α-helix | 227-237 | 11 | |
Chain E: 12 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15 | 1 | |
| β-strand | 16 | 1 | 19 |
| β-strand | 20 | 1 | 19 |
| α-helix | 22-33 | 12 | |
| α-helix | 35-36 | 2 | |
| β-strand | 37-42 | 6 | 20 |
| β-strand | 45-51 | 7 | 20 |
| β-strand | 59 | 1 | 18 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-69 | 3 | 21 |
| β-strand | 74-80 | 7 | 21 |
| α-helix | 82-103 | 22 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-120 | 12 | |
| α-helix | 121-123 | 3 | |
| α-helix | 130-132 | 3 | |
| β-strand | 140-148 | 9 | 21 |
| β-strand | 152-158 | 7 | 21 |
| β-strand | 164-166 | 3 | 21 |
| β-strand | 167 | 1 | 22 |
| β-strand | 169-172 | 4 | 20 |
| α-helix | 176-186 | 11 | |
| α-helix | 193-207 | 15 | |
| β-strand | 217-223 | 7 | 20 |
| β-strand | 227-230 | 4 | 20 |
| α-helix | 233-246 | 14 | |
Chain F: 13 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-5 | 4 | |
| α-helix | 20-27 | 8 | |
| α-helix | 28-31 | 4 | |
| α-helix | 33-34 | 2 | |
| β-strand | 35-39 | 5 | 23 |
| β-strand | 43-49 | 7 | 23 |
| β-strand | 57 | 1 | 22 |
| α-helix | 58-60 | 3 | |
| β-strand | 63-67 | 5 | 24 |
| β-strand | 70-76 | 7 | 24 |
| β-strand | 77 | 1 | 25 |
| α-helix | 78-98 | 21 | |
| α-helix | 102-104 | 3 | |
| α-helix | 105-118 | 14 | |
| β-strand | 122 | 1 | 26 |
| β-strand | 130-138 | 9 | 24 |
| β-strand | 141-147 | 7 | 24 |
| β-strand | 153-155 | 3 | 24 |
| β-strand | 156 | 1 | 27 |
| β-strand | 158-161 | 4 | 23 |
| α-helix | 165-179 | 15 | |
| α-helix | 180-182 | 3 | |
| α-helix | 186-198 | 13 | |
| α-helix | 204-206 | 3 | |
| β-strand | 211-217 | 7 | 23 |
| β-strand | 223-225 | 3 | 23 |
| α-helix | 227-233 | 7 | |
Chain G: 10 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-32 | 11 | |
| α-helix | 35-36 | 2 | |
| β-strand | 37-42 | 6 | 28 |
| β-strand | 45-53 | 9 | 28 |
| β-strand | 59 | 1 | 27 |
| β-strand | 68-71 | 4 | 29 |
| β-strand | 74-80 | 7 | 29 |
| α-helix | 82-103 | 22 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-123 | 15 | |
| β-strand | 126 | 1 | 5 |
| β-strand | 129 | 1 | 26 |
| α-helix | 130-132 | 3 | |
| β-strand | 134-140 | 7 | 29 |
| β-strand | 147-151 | 5 | 29 |
| β-strand | 157-159 | 3 | 29 |
| β-strand | 160 | 1 | 2 |
| β-strand | 162-165 | 4 | 28 |
| α-helix | 169-182 | 14 | |
| α-helix | 189-203 | 15 | |
| α-helix | 204-207 | 4 | |
| β-strand | 212-220 | 9 | 28 |
| β-strand | 229-230 | 2 | 28 |
| α-helix | 234-243 | 10 | |
Chain H: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 52-58 | 7 | |
| α-helix | 60-76 | 17 | |
| α-helix | 79-94 | 16 | |
| α-helix | 105-110 | 6 | |
| α-helix | 119-122 | 4 | |
| α-helix | 138-146 | 9 | |
5 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 |
|---|
| Proteasome subunit alpha type-1 | A | protein | 252 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P21243 (AlphaFold model) |
| Proteasome subunit alpha type-2 | B | protein | 250 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P23639 (AlphaFold model) |
| Proteasome subunit alpha type-3 | C | protein | 258 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P23638 (AlphaFold model) |
| Proteasome subunit alpha type-4 | D | protein | 254 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40303 (AlphaFold model) |
| Proteasome subunit alpha type-5 | E | protein | 260 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32379 |
| Proteasome subunit alpha type-6 | F | protein | 234 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40302 |
| Proteasome subunit alpha type-7 | G | protein | 288 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P21242 |
| Proteasome maturation factor UMP1 | H | protein | 148 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P38293 |
| Proteasome subunit beta type-2 | I | protein | 261 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P25043 |
| Proteasome subunit beta type-3 | J | protein | 205 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P25451 |
| Proteasome subunit beta type-4 | K | protein | 198 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P22141 |
| Proteasome chaperone 1 | O | protein | 276 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q05778 |
1 more molecules are not listed.
Sequence of entity 1 (A), FASTA
>7LSX_1 Proteasome subunit alpha type-1 (chains A)
MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVP
DKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKR
MANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITT
NLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAEN
IEERLVAIAEQD
Sequence of entity 2 (B), FASTA
>7LSX_2 Proteasome subunit alpha type-2 (chains B)
MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSET
LSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQE
ATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWN
DELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
Sequence of entity 3 (C), FASTA
>7LSX_3 Proteasome subunit alpha type-3 (chains C)
MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQD
TSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQ
GYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDY
KDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGITKKDEDEEADEDMK
Sequence of entity 4 (D), FASTA
>7LSX_4 Proteasome subunit alpha type-4 (chains D)
MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRIT
PSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRY
TQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYD
RKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QEQQEQDKKKKSNH
Sequence of entity 5 (E), FASTA
>7LSX_5 Proteasome subunit alpha type-5 (chains E)
MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLE
SDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLA
LRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQ
AELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAAESPEEADVEMS
Sequence of entity 6 (F), FASTA
>7LSX_6 Proteasome subunit alpha type-6 (chains F)
MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQ
KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNT
QSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFI
KIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
Sequence of entity 7 (G), FASTA
>7LSX_7 Proteasome subunit alpha type-7 (chains G)
MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLV
PQKNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYV
QAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLV
DHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAI
DFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE
Sequence of entity 8 (H), FASTA
>7LSX_8 Proteasome maturation factor UMP1 (chains H)
MNIVPQDTFKSQVSTDQDKSVLSSAVPSLPDTLRQQEGGAVPLSTQLNDRHPLESTLKNW
ETTQRQRQMEQYRQIFGIAEPMKRTMEMEIVNRTDFNPLSTNGSIHRDILLNKECSIDWE
DVYPGTGLQASTMVGDDVHSKIEKQLGI
Sequence of entity 9 (I), FASTA
>7LSX_9 Proteasome subunit beta type-2 (chains I)
MAGLSFDNYQRNNFLAENSHTQPKATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNC
AKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQ
GHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEA
IKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTA
VLKESIVNICDIQEEQVDITA
Sequence of entity 10 (J), FASTA
>7LSX_10 Proteasome subunit beta type-3 (chains J)
MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDV
TTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPF
IAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDAL
SGWGAVVYIIKKDEVVKRYLKMRQD
Sequence of entity 11 (K), FASTA
>7LSX_11 Proteasome subunit beta type-4 (chains K)
MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYI
QANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQID
YLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLLKLCVQELEKRMPMDFKGVI
VKIVDKDGIRQVDDFQAQ
Sequence of entity 12 (O), FASTA
>7LSX_12 Proteasome chaperone 1 (chains O)
MLFKQWNDLPEPKHLLDLPEISKNLQSLEVCPVPKVEFPQDLDVPQYSTAVITTKIMNPL
FPKNLLQLTSIGEIKTTLTVKSPSLPQSSGKHSWNYDENFPNEVDPDQKNDTADETVYGF
SFPIYSFGKTLLFSMEENFISISPIFGNMISRSIISQLAQFSPDIIVIGTSDKIASMKVM
TENECTLQPPEFITGFIGSVLTQLIVGPSKGLKFKCLVAPSEGPNGFEKLSLSDMGSLVD
LCGQWLGFEPSRYSEECYRLWRCDSAAIGAQSGLYI
Primary citation
Structures of chaperone-associated assembly intermediates reveal coordinated mechanisms of proteasome biogenesis. Schnell, H.M., Walsh Jr., R.M., Rawson, S. et al. Nat Struct Mol Biol (2021) 28:418-425. DOI 10.1038/s41594-021-00583-9 · PubMed
Other PDB entries of the same protein (UniProt P21243 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1RYP 1.9 Å, Crystal structure of the 20S proteasome from yeast at 2.4 Å resolution
- 8RVQ 2.02 Å, 20S proteasome from pre1-1
- 4R17 2.1 Å, Ligand-induced aziridine-formation at subunit beta5 of the yeast 20S proteasome
- 8RVL 2.14 Å, Proteasomal late precursor complex from pre1-1
- 8U7U 2.16 Å, Proteasome 20S Core Particle from Beta 3 D205 deletion
- 1G65 2.25 Å, Crystal structure of epoxomicin:20s proteasome reveals a molecular basis for selectivity…
- 8RVP 2.28 Å, Proteasomal late precursor complex from pre1-1, state 2
- 4QVP 2.3 Å, yCP beta5-M45T mutant in complex with bortezomib
- 5CZ4 2.3 Å, Yeast 20S proteasome at 2.3 A resolution
- 6HWE 2.3 Å, Yeast 20S proteasome beta2-G45A mutant in complex with carfilzomib
- 9GBK 2.39 Å, Blm10-20S proteasome complex from pre1-1
- 1G0U 2.4 Å, A gated channel into the proteasome core particle
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