6EF0: Yeast 26S proteasome
Yeast 26S proteasome bound to ubiquitinated substrate (1D* motor state). Determined by electron microscopy at 4.43 Å resolution. Released 17 Oct 2018.
- Method
- Electron microscopy
- Resolution
- 4.43 Å
- Organisms
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiens
- Chains
- 14
- Atoms
- 24,748
- Mol. weight
- 370.67 kDa
- Ligands
- ADP, ATP
- Released
- 17 Oct 2018
Explore 6EF0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6EF0 contains 142 α-helices and 147 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: 9 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-34 | 7 | |
| β-strand | 42-45 | 4 | 1 |
| β-strand | 52-55 | 4 | 1 |
| β-strand | 64 | 1 | 2 |
| β-strand | 72 | 1 | 3 |
| β-strand | 79-80 | 2 | 4 |
| β-strand | 82 | 1 | 3 |
| β-strand | 83 | 1 | 4 |
| α-helix | 88-108 | 21 | |
| α-helix | 111-113 | 3 | |
| α-helix | 114-117 | 4 | |
| α-helix | 123-127 | 5 | |
| β-strand | 131 | 1 | 5 |
| α-helix | 135-137 | 3 | |
| β-strand | 141-146 | 6 | 4 |
| β-strand | 152-157 | 6 | 4 |
| β-strand | 164-166 | 3 | 4 |
| β-strand | 171 | 1 | 1 |
| α-helix | 183-186 | 4 | |
| α-helix | 201-214 | 14 | |
| β-strand | 226 | 1 | 1 |
| β-strand | 227-229 | 3 | 6 |
| β-strand | 232-234 | 3 | 6 |
| α-helix | 239-244 | 6 | |
Chain B: 11 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-30 | 10 | |
| β-strand | 34-38 | 5 | 7 |
| β-strand | 43-48 | 6 | 7 |
| β-strand | 56 | 1 | 4 |
| β-strand | 65-68 | 4 | 8 |
| β-strand | 71-74 | 4 | 8 |
| α-helix | 83-92 | 10 | |
| α-helix | 93-99 | 7 | |
| α-helix | 100-101 | 2 | |
| α-helix | 104-105 | 2 | |
| α-helix | 110-119 | 10 | |
| β-strand | 127 | 1 | 5 |
| α-helix | 128-130 | 3 | |
| β-strand | 135-138 | 4 | 8 |
| β-strand | 146-149 | 4 | 8 |
| α-helix | 156-157 | 2 | |
| β-strand | 158 | 1 | 8 |
| β-strand | 161-164 | 4 | 7 |
| α-helix | 168-178 | 11 | |
| α-helix | 185-197 | 13 | |
| α-helix | 206-208 | 3 | |
| β-strand | 209-214 | 6 | 7 |
| β-strand | 235-237 | 3 | 7 |
Chain C: 10 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 21-28 | 8 | |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 9 |
| β-strand | 44-49 | 6 | 9 |
| β-strand | 68 | 1 | 10 |
| β-strand | 74-75 | 2 | 10 |
| β-strand | 78-79 | 2 | 11 |
| β-strand | 80 | 1 | 12 |
| α-helix | 81-83 | 3 | |
| α-helix | 87-102 | 16 | |
| α-helix | 112-122 | 11 | |
| β-strand | 125 | 1 | 13 |
| α-helix | 128-131 | 4 | |
| β-strand | 133-134 | 2 | 11 |
| β-strand | 136 | 1 | 14 |
| β-strand | 137-138 | 2 | 10 |
| β-strand | 139-140 | 2 | 15 |
| β-strand | 146-147 | 2 | 15 |
| β-strand | 149-150 | 2 | 14 |
| β-strand | 158-159 | 2 | 14 |
| β-strand | 160 | 1 | 16 |
| β-strand | 163-164 | 2 | 9 |
| α-helix | 170-176 | 7 | |
| α-helix | 190-197 | 8 | |
| α-helix | 208-210 | 3 | |
| β-strand | 212 | 1 | 9 |
| β-strand | 214-216 | 3 | 9 |
| β-strand | 228-229 | 2 | 9 |
| α-helix | 232-241 | 10 | |
Chain D: 10 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 11 | 1 | 17 |
| β-strand | 17 | 1 | 17 |
| α-helix | 18-26 | 9 | |
| α-helix | 27-29 | 3 | |
| β-strand | 33-37 | 5 | 18 |
| β-strand | 42-45 | 4 | 18 |
| β-strand | 55 | 1 | 16 |
| β-strand | 66 | 1 | 19 |
| β-strand | 72-74 | 3 | 19 |
| β-strand | 77 | 1 | 20 |
| α-helix | 82-99 | 18 | |
| α-helix | 109-119 | 11 | |
| β-strand | 126 | 1 | 13 |
| β-strand | 131 | 1 | 20 |
| β-strand | 133-136 | 4 | 19 |
| α-helix | 138-139 | 2 | |
| β-strand | 147-150 | 4 | 19 |
| β-strand | 156-158 | 3 | 19 |
| β-strand | 161-164 | 4 | 18 |
| α-helix | 172-178 | 7 | |
| α-helix | 188-199 | 12 | |
| α-helix | 200-202 | 3 | |
| β-strand | 212-215 | 4 | 18 |
| α-helix | 217-219 | 3 | |
| β-strand | 222-223 | 2 | 18 |
| α-helix | 226-238 | 13 | |
Chain E: 9 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 14-16 | 3 | |
| α-helix | 22-29 | 8 | |
| β-strand | 37-40 | 4 | 21 |
| β-strand | 46-51 | 6 | 21 |
| β-strand | 67-69 | 3 | 22 |
| β-strand | 74-77 | 4 | 22 |
| α-helix | 86-102 | 17 | |
| α-helix | 110-117 | 8 | |
| α-helix | 119-121 | 3 | |
| β-strand | 143-146 | 4 | 22 |
| β-strand | 154-155 | 2 | 22 |
| β-strand | 157 | 1 | 23 |
| β-strand | 165 | 1 | 23 |
| β-strand | 169-171 | 3 | 21 |
| α-helix | 177-184 | 8 | |
| α-helix | 193-207 | 15 | |
| β-strand | 215 | 1 | 21 |
| β-strand | 217-223 | 7 | 21 |
| β-strand | 227-230 | 4 | 21 |
| α-helix | 233-239 | 7 | |
| α-helix | 241-247 | 7 | |
Chain F: 8 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 20-31 | 12 | |
| β-strand | 35-39 | 5 | 24 |
| β-strand | 43-49 | 7 | 24 |
| β-strand | 63-67 | 5 | 25 |
| β-strand | 70-73 | 4 | 25 |
| β-strand | 76 | 1 | 26 |
| α-helix | 79-94 | 16 | |
| α-helix | 102-104 | 3 | |
| α-helix | 106-118 | 13 | |
| β-strand | 130 | 1 | 26 |
| β-strand | 133-138 | 6 | 25 |
| β-strand | 141-146 | 6 | 25 |
| β-strand | 154-155 | 2 | 25 |
| β-strand | 156 | 1 | 27 |
| β-strand | 159 | 1 | 24 |
| α-helix | 166-174 | 9 | |
| α-helix | 186-195 | 10 | |
| β-strand | 211-217 | 7 | 24 |
| β-strand | 223-225 | 3 | 24 |
| α-helix | 227-229 | 3 | |
| α-helix | 231-233 | 3 | |
Chain G: 10 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 16 | 1 | 28 |
| β-strand | 20 | 1 | 28 |
| α-helix | 27-32 | 6 | |
| β-strand | 37-41 | 5 | 29 |
| β-strand | 45-52 | 8 | 29 |
| β-strand | 59 | 1 | 27 |
| β-strand | 67-69 | 3 | 30 |
| β-strand | 75-77 | 3 | 30 |
| β-strand | 79 | 1 | 31 |
| β-strand | 81 | 1 | 31 |
| α-helix | 83-103 | 21 | |
| α-helix | 109-119 | 11 | |
| α-helix | 121-123 | 3 | |
| β-strand | 137-139 | 3 | 30 |
| β-strand | 141-142 | 2 | 32 |
| β-strand | 145-146 | 2 | 32 |
| β-strand | 149-150 | 2 | 30 |
| β-strand | 159 | 1 | 30 |
| β-strand | 160 | 1 | 2 |
| β-strand | 162 | 1 | 29 |
| α-helix | 166-168 | 3 | |
| α-helix | 169-180 | 12 | |
| α-helix | 189-203 | 15 | |
| α-helix | 204-207 | 4 | |
| β-strand | 213-216 | 4 | 29 |
| β-strand | 218 | 1 | 33 |
| β-strand | 219-220 | 2 | 29 |
| α-helix | 221-224 | 4 | |
| β-strand | 229 | 1 | 33 |
| α-helix | 234-245 | 12 | |
Chain H: 14 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 216-224 | 9 | |
| α-helix | 233-236 | 4 | |
| β-strand | 246-248 | 3 | 34 |
| α-helix | 256-264 | 9 | |
| α-helix | 266-268 | 3 | |
| β-strand | 270 | 1 | 35 |
| α-helix | 276-279 | 4 | |
| α-helix | 287-298 | 12 | |
| β-strand | 304 | 1 | 35 |
| β-strand | 305-306 | 2 | 36 |
| α-helix | 312-316 | 5 | |
| α-helix | 319-321 | 3 | |
| α-helix | 328-340 | 13 | |
| β-strand | 350-351 | 2 | 36 |
| β-strand | 373-375 | 3 | 34 |
| α-helix | 382-386 | 5 | |
| β-strand | 398 | 1 | 37 |
| α-helix | 406-409 | 4 | |
| α-helix | 419-426 | 8 | |
| α-helix | 429-433 | 5 | |
| β-strand | 438 | 1 | 37 |
| α-helix | 441-450 | 10 | |
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 | 238 | 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 | 244 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P23638 (AlphaFold model) |
| Proteasome subunit alpha type-4 | D | protein | 242 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40303 (AlphaFold model) |
| Proteasome subunit alpha type-5 | E | protein | 249 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32379 |
| Proteasome subunit alpha type-6 | F | protein | 234 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40302 |
| Probable proteasome subunit alpha type-7 | G | protein | 246 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P21242 |
| 26S proteasome regulatory subunit 7 homolog | H | protein | 257 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P33299 |
| 26S proteasome regulatory subunit 4 homolog | I | protein | 271 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40327 |
| 26S proteasome regulatory subunit 8 homolog | J | protein | 276 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q01939 |
| 26S proteasome regulatory subunit 6B homolog | K | protein | 272 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P33298 |
| 26S proteasome subunit RPT4 | L | protein | 273 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P53549 |
2 more molecules are not listed.
Sequence of entity 1 (A), FASTA
>6EF0_1 Proteasome subunit alpha type-1 (chains A)
GYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVS
YIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQ
RAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKKSK
IDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAENIEERLVAI
Sequence of entity 2 (B), FASTA
>6EF0_2 Proteasome subunit alpha type-2 (chains B)
MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSET
LSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQE
ATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWN
DELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
Sequence of entity 3 (C), FASTA
>6EF0_3 Proteasome subunit alpha type-3 (chains C)
MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQD
TSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQ
GYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDY
KDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILV
KTGI
Sequence of entity 4 (D), FASTA
>6EF0_4 Proteasome subunit alpha type-4 (chains D)
MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRIT
PSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRY
TQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYD
RKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEK
QE
Sequence of entity 5 (E), FASTA
>6EF0_5 Proteasome subunit alpha type-5 (chains E)
MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLE
SDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLA
LRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQ
AELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELI
KELKEKEAA
Sequence of entity 6 (F), FASTA
>6EF0_6 Proteasome subunit alpha type-6 (chains F)
MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQ
KKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNT
QSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFI
KIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
Sequence of entity 7 (G), FASTA
>6EF0_7 Probable proteasome subunit alpha type-7 (chains G)
SIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQ
KNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQA
HTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLVDH
HPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAIDF
AQKEIN
Sequence of entity 8 (H), FASTA
>6EF0_8 26S proteasome regulatory subunit 7 homolog (chains H)
EEKPDVTYSDVGGCKDQIEKLREVVELPLLSPERFATLGIDPPKGILLYGPPGTGKTLCA
RAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDAVGGARFD
DGAGGDNEVQRTMLELITQLDGFDPRGNIKVMFATNRPNTLDPALLRPGRIDRKVEFSLP
DLEGRANIFRIHSKSMSVERGIRWELISRLCPNSTGAELRSVCTEAGMFAIRARRKVATE
KDFLKAVDKVISGYKKF
Sequence of entity 9 (I), FASTA
>6EF0_9 26S proteasome regulatory subunit 4 homolog (chains I)
PMVSVMKMDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAP
GTGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAGENAPSIVFIDEID
AIGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIETLDPALIRPGRID
RKILFENPDLSTKKKILGIHTSKMNLSEDVNLETLVTTKDDLSGADIQAMCTEAGLLALR
ERRMQVTAEDFKQAKERVMKNKVEENLEGLY
Sequence of entity 10 (J), FASTA
>6EF0_10 26S proteasome regulatory subunit 8 homolog (chains J)
ADPLVSLMMVEKVPDSTYDMVGGLTKQIKEIKEVIELPVKHPELFESLGIAQPKGVILYG
PPGTGKTLLARAVAHHTDCKFIRVSGAELVQKYIGEGSRMVRELFVMAREHAPSIIFMDE
IDSIGSTRVEGSGGGDSEVQRTMLELLNQLDGFETSKNIKIIMATNRLDILDPALLRPGR
IDRKIEFPPPSVAARAEILRIHSRKMNLTRGINLRKVAEKMNGCSGADVKGVCTEAGMYA
LRERRIHVTQEDFELAVGKVMNKNQETAISVAKLFK
Sequence of entity 11 (K), FASTA
>6EF0_11 26S proteasome regulatory subunit 6B homolog (chains K)
SISVMGENEKPDVTYADVGGLDMQKQEIREAVELPLVQADLYEQIGIDPPRGVLLYGPPG
TGKTMLVKAVANSTKAAFIRVNGSEFVHKYLGEGPRMVRDVFRLARENAPSIIFIDEVDS
IATKRFDAQTGSDREVQRILIELLTQMDGFDQSTNVKVIMATNRADTLDPALLRPGRLDR
KIEFPSLRDRRERRLIFGTIASKMSLAPEADLDSLIIRNDSLSGAVIAAIMQEAGLRAVR
KNRYVILQSDLEEAYATQVKTDNTVDKFDFYK
Sequence of entity 12 (L), FASTA
>6EF0_12 26S proteasome subunit RPT4 (chains L)
DPLVYNMTSFEQGEITFDGIGGLTEQIRELREVIELPLKNPEIFQRVGIKPPKGVLLYGP
PGTGKTLLAKAVAATIGANFIFSPASGIVDKYIGESARIIREMFAYAKEHEPCIIFMDEV
DAIGGRRFSEGTSADREIQRTLMELLTQMDGFDNLGQTKIIMATNRPDTLDPALLRPGRL
DRKVEIPLPNEAGRLEIFKIHTAKVKKTGEFDFEAAVKMSDGFNGADIRNCATEAGFFAI
RDDRDHINPDDLMKAVRKVAEVKKLEGTIEYQK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 3 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 3 |
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 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
Browse structure collections
About this viewer
MolViewer shows 6EF0 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.