6EF3: Yeast 26S proteasome
Yeast 26S proteasome bound to ubiquitinated substrate (4D motor state). Determined by electron microscopy at 4.17 Å resolution. Released 17 Oct 2018.
- Method
- Electron microscopy
- Resolution
- 4.17 Å
- Organisms
- Saccharomyces cerevisiae S288c, Homo sapiens
- Chains
- 24
- Atoms
- 44,271
- Mol. weight
- 733.22 kDa
- Ligands
- ADP, ATP
- Released
- 17 Oct 2018
Explore 6EF3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6EF3 contains 227 α-helices and 289 β-strands across 23 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 1: 5 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-8 | 6 | 1 |
| β-strand | 11-18 | 8 | 1 |
| β-strand | 22 | 1 | 2 |
| β-strand | 25 | 1 | 2 |
| β-strand | 38 | 1 | 3 |
| β-strand | 41-47 | 7 | 3 |
| α-helix | 50-69 | 20 | |
| α-helix | 76-86 | 11 | |
| β-strand | 95-101 | 7 | 3 |
| β-strand | 109 | 1 | 3 |
| β-strand | 111-113 | 3 | 3 |
| β-strand | 120-121 | 2 | 3 |
| β-strand | 124-127 | 4 | 1 |
| α-helix | 135-139 | 5 | |
| α-helix | 148-164 | 17 | |
| β-strand | 172-179 | 8 | 1 |
| β-strand | 183 | 1 | 1 |
| β-strand | 186-188 | 3 | 1 |
| α-helix | 190-194 | 5 | |
Chain 2: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-8 | 6 | 4 |
| β-strand | 11-17 | 7 | 4 |
| β-strand | 34-35 | 2 | 5 |
| β-strand | 42-45 | 4 | 5 |
| α-helix | 49-62 | 14 | |
| α-helix | 64-70 | 7 | |
| α-helix | 78-81 | 4 | |
| α-helix | 83-90 | 8 | |
| β-strand | 98-104 | 7 | 5 |
| β-strand | 107-113 | 7 | 5 |
| β-strand | 120 | 1 | 5 |
| β-strand | 124-127 | 4 | 4 |
| α-helix | 131-139 | 9 | |
| α-helix | 148-164 | 17 | |
| β-strand | 173-177 | 5 | 4 |
| β-strand | 185-191 | 7 | 4 |
| β-strand | 215-218 | 4 | 6 |
Chain 3: 5 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-6 | 3 | |
| β-strand | 11-17 | 7 | 6 |
| β-strand | 20-26 | 7 | 6 |
| β-strand | 29 | 1 | 7 |
| β-strand | 37 | 1 | 7 |
| β-strand | 43-46 | 4 | 8 |
| β-strand | 49-52 | 4 | 8 |
| α-helix | 58-78 | 21 | |
| α-helix | 84-96 | 13 | |
| β-strand | 108-113 | 6 | 8 |
| β-strand | 118-123 | 6 | 8 |
| β-strand | 131 | 1 | 8 |
| β-strand | 136-140 | 5 | 6 |
| α-helix | 148-151 | 4 | |
| α-helix | 160-175 | 16 | |
| β-strand | 185-190 | 6 | 6 |
| β-strand | 195-200 | 6 | 6 |
Chain 4: 5 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 9 |
| β-strand | 13-15 | 3 | 9 |
| β-strand | 22-23 | 2 | 10 |
| β-strand | 26-27 | 2 | 10 |
| β-strand | 35-39 | 5 | 11 |
| β-strand | 42-48 | 7 | 11 |
| α-helix | 54-68 | 15 | |
| α-helix | 77-91 | 15 | |
| β-strand | 100-107 | 8 | 11 |
| β-strand | 114-119 | 6 | 11 |
| β-strand | 126 | 1 | 11 |
| β-strand | 130-132 | 3 | 9 |
| α-helix | 137-139 | 3 | |
| α-helix | 154-161 | 8 | |
| α-helix | 164-169 | 6 | |
| β-strand | 182-184 | 3 | 9 |
| β-strand | 190-191 | 2 | 9 |
Chain 5: 6 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-7 | 6 | 12 |
| β-strand | 12-16 | 5 | 12 |
| β-strand | 20-22 | 3 | 13 |
| β-strand | 25-28 | 4 | 13 |
| β-strand | 34-38 | 5 | 14 |
| β-strand | 41-44 | 4 | 14 |
| β-strand | 47 | 1 | 15 |
| α-helix | 49-64 | 16 | |
| α-helix | 67-70 | 4 | |
| α-helix | 76-88 | 13 | |
| β-strand | 97 | 1 | 15 |
| β-strand | 98-104 | 7 | 14 |
| β-strand | 110-116 | 7 | 14 |
| β-strand | 123 | 1 | 14 |
| β-strand | 126-130 | 5 | 12 |
| α-helix | 133-143 | 11 | |
| α-helix | 151-162 | 12 | |
| β-strand | 174-181 | 8 | 12 |
| β-strand | 184-192 | 9 | 12 |
| α-helix | 193-204 | 12 | |
Chain 6: 6 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 11-15 | 5 | 16 |
| β-strand | 16 | 1 | 17 |
| β-strand | 21 | 1 | 17 |
| β-strand | 24-25 | 2 | 16 |
| β-strand | 29-30 | 2 | 18 |
| β-strand | 35-37 | 3 | 18 |
| β-strand | 43-45 | 3 | 19 |
| β-strand | 51-56 | 6 | 19 |
| α-helix | 60-79 | 20 | |
| α-helix | 86-98 | 13 | |
| β-strand | 107-114 | 8 | 19 |
| β-strand | 120-124 | 5 | 19 |
| β-strand | 132-134 | 3 | 19 |
| β-strand | 136-140 | 5 | 16 |
| α-helix | 147-150 | 4 | |
| β-strand | 160 | 1 | 20 |
| α-helix | 168 | 1 | |
| β-strand | 169 | 1 | 20 |
| α-helix | 170 | 1 | |
| α-helix | 177-187 | 11 | |
| β-strand | 202-204 | 3 | 16 |
| β-strand | 207-208 | 2 | 17 |
| β-strand | 211-212 | 2 | 17 |
| β-strand | 215-217 | 3 | 16 |
Chain 7: 6 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7 | 1 | 21 |
| β-strand | 11-15 | 5 | 22 |
| β-strand | 19-24 | 6 | 22 |
| β-strand | 28-29 | 2 | 23 |
| β-strand | 34-36 | 3 | 23 |
| β-strand | 42 | 1 | 24 |
| β-strand | 45 | 1 | 24 |
| β-strand | 49-52 | 4 | 24 |
| β-strand | 56 | 1 | 21 |
| α-helix | 57-75 | 19 | |
| α-helix | 90-93 | 4 | |
| α-helix | 95-104 | 10 | |
| β-strand | 114-119 | 6 | 24 |
| β-strand | 125-130 | 6 | 24 |
| β-strand | 136-137 | 2 | 24 |
| β-strand | 143 | 1 | 22 |
| α-helix | 146-150 | 5 | |
| α-helix | 152-158 | 7 | |
| α-helix | 170-187 | 18 | |
| β-strand | 196-201 | 6 | 22 |
| β-strand | 205-208 | 4 | 22 |
Chain A: 12 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-9 | 5 | |
| α-helix | 28-30 | 3 | |
| α-helix | 32-34 | 3 | |
| β-strand | 43-45 | 3 | 25 |
| β-strand | 51-56 | 6 | 25 |
| β-strand | 64 | 1 | 26 |
| β-strand | 72-73 | 2 | 27 |
| β-strand | 79-82 | 4 | 27 |
| α-helix | 88-98 | 11 | |
| α-helix | 101-107 | 7 | |
| α-helix | 114-120 | 7 | |
| α-helix | 122-125 | 4 | |
| α-helix | 127-129 | 3 | |
| α-helix | 135-137 | 3 | |
| β-strand | 141-147 | 7 | 27 |
| β-strand | 151-157 | 7 | 27 |
| β-strand | 166 | 1 | 28 |
| β-strand | 168-170 | 3 | 25 |
| α-helix | 175-189 | 15 | |
| α-helix | 199-212 | 14 | |
| β-strand | 223-229 | 7 | 25 |
| β-strand | 232-235 | 4 | 25 |
| α-helix | 242-245 | 4 | |
15 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 beta type-1 | 1 | protein | 215 | Saccharomyces cerevisiae S288c | P38624 (AlphaFold model) |
| Proteasome subunit beta type-2 | 2 | protein | 261 | Saccharomyces cerevisiae S288c | P25043 (AlphaFold model) |
| Proteasome subunit beta type-3 | 3 | protein | 205 | Saccharomyces cerevisiae S288c | P25451 (AlphaFold model) |
| Proteasome subunit beta type-4 | 4 | protein | 198 | Saccharomyces cerevisiae S288c | P22141 (AlphaFold model) |
| Proteasome subunit beta type-5 | 5 | protein | 287 | Saccharomyces cerevisiae S288c | P30656 |
| Proteasome subunit beta type-6 | 6 | protein | 241 | Saccharomyces cerevisiae S288c | P23724 |
| Proteasome subunit beta type-7 | 7 | protein | 266 | Saccharomyces cerevisiae S288c | P30657 |
| Proteasome subunit alpha type-1 | A | protein | 252 | Saccharomyces cerevisiae S288c | P21243 |
| Proteasome subunit alpha type-2 | B | protein | 250 | Saccharomyces cerevisiae S288c | P23639 |
| Proteasome subunit alpha type-3 | C | protein | 258 | Saccharomyces cerevisiae S288c | P23638 |
| Proteasome subunit alpha type-4 | D | protein | 254 | Saccharomyces cerevisiae S288c | P40303 |
| Proteasome subunit alpha type-5 | E | protein | 260 | Saccharomyces cerevisiae S288c | P32379 |
12 more molecules are not listed.
Sequence of entity 1 (1), FASTA
>6EF3_1 Proteasome subunit beta type-1 (chains 1)
MNGIQVDINRLKKGEVSLGTSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKI
WCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVAG
YDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLSQ
AIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
Sequence of entity 2 (2), FASTA
>6EF3_2 Proteasome subunit beta type-2 (chains 2)
MAGLSFDNYQRNNFLAENSHTQPKATSTGTTIVGVKFNNGVVIAADTRSTQGPIVADKNC
AKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQ
GHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEA
IKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTA
VLKESIVNICDIQEEQVDITA
Sequence of entity 3 (3), FASTA
>6EF3_3 Proteasome subunit beta type-3 (chains 3)
MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDV
TTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPF
IAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDAL
SGWGAVVYIIKKDEVVKRYLKMRQD
Sequence of entity 4 (4), FASTA
>6EF3_4 Proteasome subunit beta type-4 (chains 4)
MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYI
QANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQID
YLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLLKLCVQELEKRMPMDFKGVI
VKIVDKDGIRQVDDFQAQ
Sequence of entity 5 (5), FASTA
>6EF3_5 Proteasome subunit beta type-5 (chains 5)
MQAIADSFSVPNRLVKELQYDNEQNLESDFVTGASQFQRLAPSLTVPPIASPQQFLRAHT
DDSRNPDCKIKIAHGTTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTM
AGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYT
RKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAA
HRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG
Sequence of entity 6 (6), FASTA
>6EF3_6 Proteasome subunit beta type-6 (chains 6)
MATIASEYSSEASNTPIEHQFNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEP
KVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDKKLSINSAARNIQHLLYGKR
FFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQYE
PGTNGKVKKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKR
D
Sequence of entity 7 (7), FASTA
>6EF3_7 Proteasome subunit beta type-7 (chains 7)
MNHDPFSWGRPADSTYGAYNTQIANAGASPMVNTQQPIVTGTSVISMKYDNGVIIAADNL
GSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLKDLVTENAYDNPLADAEEAL
EPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFG
AHMANPLLRKVVDRESDIPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKNTGLT
FKKNLQVENMKWDFAKDIKGYGTQKI
Sequence of entity 8 (A), FASTA
>6EF3_8 Proteasome subunit alpha type-1 (chains A)
MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVP
DKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKR
MANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITT
NLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAEN
IEERLVAIAEQD
Sequence of entity 9 (B), FASTA
>6EF3_9 Proteasome subunit alpha type-2 (chains B)
MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSET
LSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQE
ATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWN
DELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
Sequence of entity 10 (C), FASTA
>6EF3_10 Proteasome subunit alpha type-3 (chains C)
MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQD
TSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQ
GYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDY
KDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGITKKDEDEEADEDMK
Sequence of entity 11 (D), FASTA
>6EF3_11 Proteasome subunit alpha type-4 (chains D)
MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRIT
PSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRY
TQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYD
RKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QEQQEQDKKKKSNH
Sequence of entity 12 (E), FASTA
>6EF3_12 Proteasome subunit alpha type-5 (chains E)
MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLE
SDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLA
LRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQ
AELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAAESPEEADVEMS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 4 |
Primary citation
Substrate-engaged 26Sproteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation. de la Pena, A.H., Goodall, E.A., Gates, S.N. et al. Science (2018) 362. DOI 10.1126/science.aav0725 · PubMed
Other PDB entries of the same protein (UniProt P38624 (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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