6EF1: Yeast 26S proteasome
Yeast 26S proteasome bound to ubiquitinated substrate (5D motor state). Determined by electron microscopy at 4.73 Å resolution. Released 17 Oct 2018.
- Method
- Electron microscopy
- Resolution
- 4.73 Å
- Organisms
- Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiens
- Chains
- 14
- Atoms
- 23,658
- Mol. weight
- 369.08 kDa
- Ligands
- ATP, ADP
- Released
- 17 Oct 2018
Explore 6EF1 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6EF1 contains 152 α-helices and 142 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, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-20 | 2 | |
| α-helix | 26-35 | 10 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 51-56 | 6 | 1 |
| β-strand | 64 | 1 | 2 |
| β-strand | 80 | 1 | 3 |
| β-strand | 83 | 1 | 3 |
| α-helix | 87-108 | 22 | |
| α-helix | 114-129 | 16 | |
| β-strand | 131 | 1 | 4 |
| β-strand | 141-145 | 5 | 3 |
| β-strand | 153-157 | 5 | 3 |
| β-strand | 163-164 | 2 | 3 |
| β-strand | 169-171 | 3 | 1 |
| α-helix | 175-189 | 15 | |
| α-helix | 199-201 | 3 | |
| α-helix | 203-213 | 11 | |
| α-helix | 215-217 | 3 | |
| β-strand | 223-229 | 7 | 1 |
| β-strand | 232-235 | 4 | 1 |
| α-helix | 238-245 | 8 | |
| α-helix | 246-249 | 4 | |
Chain B: 12 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8 | 1 | 5 |
| β-strand | 13 | 1 | 6 |
| β-strand | 16 | 1 | 6 |
| α-helix | 19-22 | 4 | |
| α-helix | 24-30 | 7 | |
| β-strand | 34-37 | 4 | 7 |
| β-strand | 43-47 | 5 | 7 |
| β-strand | 64-68 | 5 | 8 |
| β-strand | 71-74 | 4 | 8 |
| β-strand | 77 | 1 | 9 |
| α-helix | 80-92 | 13 | |
| α-helix | 93-98 | 6 | |
| α-helix | 99-101 | 3 | |
| α-helix | 104-105 | 2 | |
| α-helix | 107-118 | 12 | |
| α-helix | 120-123 | 4 | |
| β-strand | 125 | 1 | 5 |
| β-strand | 127 | 1 | 4 |
| β-strand | 132 | 1 | 9 |
| β-strand | 135-137 | 3 | 8 |
| β-strand | 147-150 | 4 | 8 |
| β-strand | 156-159 | 4 | 8 |
| β-strand | 161-164 | 4 | 7 |
| α-helix | 168-178 | 11 | |
| α-helix | 188-198 | 11 | |
| β-strand | 211-214 | 4 | 7 |
| α-helix | 219-222 | 4 | |
| β-strand | 235-237 | 3 | 7 |
| α-helix | 240-248 | 9 | |
Chain C: 10 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-28 | 7 | |
| α-helix | 29-31 | 3 | |
| β-strand | 34-38 | 5 | 10 |
| β-strand | 44-49 | 6 | 10 |
| β-strand | 68-70 | 3 | 11 |
| β-strand | 73-74 | 2 | 11 |
| β-strand | 76-79 | 4 | 12 |
| β-strand | 80 | 1 | 13 |
| α-helix | 85-102 | 18 | |
| α-helix | 105-107 | 3 | |
| α-helix | 108-111 | 4 | |
| α-helix | 117-123 | 7 | |
| β-strand | 125 | 1 | 14 |
| β-strand | 133-136 | 4 | 12 |
| β-strand | 139-141 | 3 | 15 |
| β-strand | 145-147 | 3 | 15 |
| β-strand | 149 | 1 | 16 |
| β-strand | 150 | 1 | 12 |
| β-strand | 159 | 1 | 16 |
| β-strand | 162-163 | 2 | 10 |
| α-helix | 169-179 | 11 | |
| α-helix | 186-200 | 15 | |
| α-helix | 208-210 | 3 | |
| β-strand | 211-216 | 6 | 10 |
| β-strand | 217 | 1 | 17 |
| β-strand | 226 | 1 | 17 |
| α-helix | 232-241 | 10 | |
Chain D: 9 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 18-23 | 6 | |
| β-strand | 34-37 | 4 | 18 |
| β-strand | 42-47 | 6 | 18 |
| β-strand | 64-66 | 3 | 19 |
| β-strand | 72-75 | 4 | 19 |
| α-helix | 80-99 | 20 | |
| α-helix | 107-119 | 13 | |
| β-strand | 126 | 1 | 14 |
| β-strand | 133-136 | 4 | 19 |
| β-strand | 137-138 | 2 | 20 |
| α-helix | 139 | 1 | |
| β-strand | 145-146 | 2 | 20 |
| β-strand | 149 | 1 | 19 |
| β-strand | 157 | 1 | 19 |
| β-strand | 161-163 | 3 | 18 |
| α-helix | 168-174 | 7 | |
| α-helix | 175-177 | 3 | |
| β-strand | 180 | 1 | 21 |
| β-strand | 183 | 1 | 21 |
| α-helix | 188-203 | 16 | |
| α-helix | 207-209 | 3 | |
| β-strand | 210-215 | 6 | 18 |
| β-strand | 222 | 1 | 18 |
| α-helix | 226-237 | 12 | |
Chain E: 9 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 23-27 | 5 | |
| α-helix | 31-33 | 3 | |
| β-strand | 37-38 | 2 | 22 |
| β-strand | 39-40 | 2 | 23 |
| β-strand | 41-42 | 2 | 24 |
| β-strand | 45-46 | 2 | 24 |
| β-strand | 49-50 | 2 | 22 |
| β-strand | 67 | 1 | 25 |
| β-strand | 74-79 | 6 | 25 |
| α-helix | 82-102 | 21 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-119 | 11 | |
| α-helix | 120-122 | 3 | |
| β-strand | 141-146 | 6 | 25 |
| β-strand | 148 | 1 | 26 |
| β-strand | 152 | 1 | 26 |
| β-strand | 156-159 | 4 | 25 |
| β-strand | 163-166 | 4 | 25 |
| β-strand | 169-170 | 2 | 23 |
| α-helix | 176-185 | 10 | |
| α-helix | 194-204 | 11 | |
| β-strand | 220-223 | 4 | 24 |
| β-strand | 227-230 | 4 | 24 |
| α-helix | 233-247 | 15 | |
Chain F: 11 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 20-25 | 6 | |
| α-helix | 27-31 | 5 | |
| β-strand | 37-38 | 2 | 27 |
| β-strand | 39 | 1 | 28 |
| β-strand | 43-49 | 7 | 28 |
| β-strand | 52 | 1 | 29 |
| β-strand | 59 | 1 | 29 |
| β-strand | 63-67 | 5 | 30 |
| β-strand | 70-75 | 6 | 30 |
| β-strand | 77 | 1 | 31 |
| α-helix | 79-93 | 15 | |
| α-helix | 95-99 | 5 | |
| α-helix | 105-120 | 16 | |
| β-strand | 131-138 | 8 | 30 |
| β-strand | 141-145 | 5 | 30 |
| β-strand | 155-156 | 2 | 30 |
| β-strand | 158-159 | 2 | 27 |
| α-helix | 166-173 | 8 | |
| α-helix | 179-181 | 3 | |
| α-helix | 186-197 | 12 | |
| α-helix | 198-200 | 3 | |
| β-strand | 211-217 | 7 | 28 |
| α-helix | 220-222 | 3 | |
| β-strand | 223-225 | 3 | 28 |
| α-helix | 229-232 | 4 | |
Chain G: 11 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-31 | 10 | |
| β-strand | 37-41 | 5 | 32 |
| β-strand | 45-50 | 6 | 32 |
| β-strand | 53-54 | 2 | 33 |
| β-strand | 59 | 1 | 30 |
| α-helix | 60 | 1 | |
| β-strand | 68 | 1 | 34 |
| β-strand | 74-80 | 7 | 34 |
| α-helix | 84-95 | 12 | |
| α-helix | 97-103 | 7 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-114 | 6 | |
| α-helix | 119-122 | 4 | |
| β-strand | 134-141 | 8 | 34 |
| β-strand | 146-151 | 6 | 34 |
| β-strand | 157-158 | 2 | 34 |
| β-strand | 160 | 1 | 2 |
| β-strand | 162-164 | 3 | 32 |
| α-helix | 169-180 | 12 | |
| α-helix | 189-203 | 15 | |
| α-helix | 204-207 | 4 | |
| β-strand | 211-212 | 2 | 33 |
| β-strand | 215-220 | 6 | 32 |
| β-strand | 229-230 | 2 | 32 |
| α-helix | 234-247 | 14 | |
Chain H: 11 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 219-230 | 12 | |
| α-helix | 232-238 | 7 | |
| β-strand | 245-246 | 2 | 35 |
| β-strand | 248-249 | 2 | 36 |
| α-helix | 256-267 | 12 | |
| α-helix | 276-279 | 4 | |
| α-helix | 288-298 | 11 | |
| β-strand | 306 | 1 | 35 |
| α-helix | 329-343 | 15 | |
| β-strand | 351-352 | 2 | 35 |
| β-strand | 375-376 | 2 | 36 |
| α-helix | 379-381 | 3 | |
| α-helix | 382-392 | 11 | |
| β-strand | 398 | 1 | 37 |
| α-helix | 405-408 | 4 | |
| α-helix | 417-433 | 17 | |
| β-strand | 438 | 1 | 37 |
| α-helix | 441-452 | 12 | |
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 | 239 | 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 | 238 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P23638 (AlphaFold model) |
| Proteasome subunit alpha type-4 | D | protein | 234 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40303 (AlphaFold model) |
| Proteasome subunit alpha type-5 | E | protein | 242 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P32379 |
| Proteasome subunit alpha type-6 | F | protein | 233 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P40302 |
| Probable proteasome subunit alpha type-7 | G | protein | 243 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P21242 |
| 26S proteasome regulatory subunit 7 homolog | H | protein | 262 | 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 | 273 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q01939 |
| 26S proteasome regulatory subunit 6B homolog | K | protein | 276 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P33298 |
| 26S proteasome subunit RPT4 | L | protein | 271 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P53549 |
2 more molecules are not listed.
Sequence of entity 1 (A), FASTA
>6EF1_1 Proteasome subunit alpha type-1 (chains A)
DRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYI
FCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRA
YMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKKSKID
HINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAENIEERLVAIAEQ
Sequence of entity 2 (B), FASTA
>6EF1_2 Proteasome subunit alpha type-2 (chains B)
MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSET
LSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQE
ATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWN
DELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTS
QEINDRLEAL
Sequence of entity 3 (C), FASTA
>6EF1_3 Proteasome subunit alpha type-3 (chains C)
SRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQDTSTEKLY
KLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQGYTQHGG
LRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDYKDDMKVD
DAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILVKTGIT
Sequence of entity 4 (D), FASTA
>6EF1_4 Proteasome subunit alpha type-4 (chains D)
SIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKID
SHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRP
FGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYDRKEPPATV
EECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEKQE
Sequence of entity 5 (E), FASTA
>6EF1_5 Proteasome subunit alpha type-5 (chains E)
DRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIV
EIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGAS
GEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWH
SSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELIKELKEKEA
AE
Sequence of entity 6 (F), FASTA
>6EF1_6 Proteasome subunit alpha type-6 (chains F)
FRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQK
KIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQ
SYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFIK
IDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI
Sequence of entity 7 (G), FASTA
>6EF1_7 Probable proteasome subunit alpha type-7 (chains G)
TGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNV
KIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTL
YNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLVDHHPE
GLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAIDFAQK
EIN
Sequence of entity 8 (H), FASTA
>6EF1_8 26S proteasome regulatory subunit 7 homolog (chains H)
SVTMMTVEEKPDVTYSDVGGCKDQIEKLREVVELPLLSPERFATLGIDPPKGILLYGPPG
TGKTLCARAVANRTDATFIRVIGSELVQKYVGEGARMVRELFEMARTKKACIIFFDEIDA
VGGARFDDGAGGDNEVQRTMLELITQLDGFDPRGNIKVMFATNRPNTLDPALLRPGRIDR
KVEFSLPDLEGRANIFRIHSKSMSVERGIRWELISRLCPNSTGAELRSVCTEAGMFAIRA
RRKVATEKDFLKAVDKVISGYK
Sequence of entity 9 (I), FASTA
>6EF1_9 26S proteasome regulatory subunit 4 homolog (chains I)
MVSVMKMDKSPTESYSDIGGLESQIQEIKESVELPLTHPELYEEMGIKPPKGVILYGAPG
TGKTLLAKAVANQTSATFLRIVGSELIQKYLGDGPRLCRQIFKVAGENAPSIVFIDEIDA
IGTKRYDSNSGGEREIQRTMLELLNQLDGFDDRGDVKVIMATNKIETLDPALIRPGRIDR
KILFENPDLSTKKKILGIHTSKMNLSEDVNLETLVTTKDDLSGADIQAMCTEAGLLALRE
RRMQVTAEDFKQAKERVMKNKVEENLEGLYL
Sequence of entity 10 (J), FASTA
>6EF1_10 26S proteasome regulatory subunit 8 homolog (chains J)
LVSLMMVEKVPDSTYDMVGGLTKQIKEIKEVIELPVKHPELFESLGIAQPKGVILYGPPG
TGKTLLARAVAHHTDCKFIRVSGAELVQKYIGEGSRMVRELFVMAREHAPSIIFMDEIDS
IGSTRVEGSGGGDSEVQRTMLELLNQLDGFETSKNIKIIMATNRLDILDPALLRPGRIDR
KIEFPPPSVAARAEILRIHSRKMNLTRGINLRKVAEKMNGCSGADVKGVCTEAGMYALRE
RRIHVTQEDFELAVGKVMNKNQETAISVAKLFK
Sequence of entity 11 (K), FASTA
>6EF1_11 26S proteasome regulatory subunit 6B homolog (chains K)
DSDSSISVMGENEKPDVTYADVGGLDMQKQEIREAVELPLVQADLYEQIGIDPPRGVLLY
GPPGTGKTMLVKAVANSTKAAFIRVNGSEFVHKYLGEGPRMVRDVFRLARENAPSIIFID
EVDSIATKRFDAQTGSDREVQRILIELLTQMDGFDQSTNVKVIMATNRADTLDPALLRPG
RLDRKIEFPSLRDRRERRLIFGTIASKMSLAPEADLDSLIIRNDSLSGAVIAAIMQEAGL
RAVRKNRYVILQSDLEEAYATQVKTDNTVDKFDFYK
Sequence of entity 12 (L), FASTA
>6EF1_12 26S proteasome subunit RPT4 (chains L)
LVYNMTSFEQGEITFDGIGGLTEQIRELREVIELPLKNPEIFQRVGIKPPKGVLLYGPPG
TGKTLLAKAVAATIGANFIFSPASGIVDKYIGESARIIREMFAYAKEHEPCIIFMDEVDA
IGGRRFSEGTSADREIQRTLMELLTQMDGFDNLGQTKIIMATNRPDTLDPALLRPGRLDR
KVEIPLPNEAGRLEIFKIHTAKVKKTGEFDFEAAVKMSDGFNGADIRNCATEAGFFAIRD
DRDHINPDDLMKAVRKVAEVKKLEGTIEYQK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 4 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
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
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