3JCK: Yeast 26S proteasome lid sub-complex
Structure of the yeast 26S proteasome lid sub-complex. Determined by electron microscopy at 3.5 Å resolution. Released 20 Jan 2016.
- Method
- Electron microscopy
- Resolution
- 3.5 Å
- Organism
- Saccharomyces cerevisiae S288c
- Chains
- 9
- Atoms
- 22,457
- Mol. weight
- 361.33 kDa
- Ligands
- ZN
- Released
- 20 Jan 2016
Explore 3JCK in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3JCK contains 160 α-helices and 41 β-strands across 9 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: 24 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 29-36 | 8 | |
| α-helix | 44-54 | 11 | |
| α-helix | 61-70 | 10 | |
| α-helix | 132-149 | 18 | |
| α-helix | 153-158 | 6 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-172 | 9 | |
| α-helix | 175-195 | 21 | |
| α-helix | 201-224 | 24 | |
| α-helix | 227-243 | 17 | |
| α-helix | 248-255 | 8 | |
| α-helix | 266-282 | 17 | |
| α-helix | 289-298 | 10 | |
| α-helix | 307-323 | 17 | |
| α-helix | 327-329 | 3 | |
| α-helix | 330-333 | 4 | |
| α-helix | 337-340 | 4 | |
| α-helix | 343-354 | 12 | |
| α-helix | 357-372 | 16 | |
| α-helix | 376-380 | 5 | |
| α-helix | 384-397 | 14 | |
| β-strand | 401-403 | 3 | 1 |
| α-helix | 404-410 | 7 | |
| α-helix | 416-428 | 13 | |
| β-strand | 434-437 | 4 | 1 |
| β-strand | 442-445 | 4 | 1 |
| α-helix | 456-477 | 22 | |
Chain B: 28 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 32-35 | 4 | |
| α-helix | 37-41 | 5 | |
| α-helix | 42-44 | 3 | |
| α-helix | 49-69 | 21 | |
| α-helix | 72-84 | 13 | |
| α-helix | 94-106 | 13 | |
| α-helix | 111-125 | 15 | |
| α-helix | 135-141 | 7 | |
| α-helix | 142-146 | 5 | |
| α-helix | 147 | 1 | |
| α-helix | 153-160 | 8 | |
| α-helix | 165-167 | 3 | |
| α-helix | 173-190 | 18 | |
| α-helix | 194-201 | 8 | |
| α-helix | 205-209 | 5 | |
| α-helix | 211-231 | 21 | |
| α-helix | 235-245 | 11 | |
| α-helix | 248-252 | 5 | |
| α-helix | 254-270 | 17 | |
| α-helix | 272 | 1 | |
| α-helix | 275-286 | 12 | |
| α-helix | 288-291 | 4 | |
| α-helix | 295-304 | 10 | |
| α-helix | 311-324 | 14 | |
| α-helix | 337-356 | 20 | |
| β-strand | 357-361 | 5 | 2 |
| α-helix | 362-369 | 8 | |
| α-helix | 373-385 | 13 | |
| β-strand | 392-394 | 3 | 2 |
| β-strand | 399-401 | 3 | 2 |
| α-helix | 408-439 | 32 | |
Chain C: 22 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 55-57 | 3 | |
| α-helix | 59-64 | 6 | |
| α-helix | 71-83 | 13 | |
| α-helix | 94-105 | 12 | |
| α-helix | 112-127 | 16 | |
| α-helix | 131-144 | 14 | |
| α-helix | 152-168 | 17 | |
| α-helix | 171-187 | 17 | |
| α-helix | 192-207 | 16 | |
| α-helix | 212-228 | 17 | |
| α-helix | 232-248 | 17 | |
| α-helix | 254-272 | 19 | |
| α-helix | 276-281 | 6 | |
| α-helix | 284-288 | 5 | |
| α-helix | 289-291 | 3 | |
| α-helix | 294-308 | 15 | |
| α-helix | 311-316 | 6 | |
| α-helix | 322-325 | 4 | |
| α-helix | 329-351 | 23 | |
| β-strand | 354-355 | 2 | 2 |
| α-helix | 359-366 | 8 | |
| α-helix | 370-382 | 13 | |
| β-strand | 388-391 | 4 | 3 |
| β-strand | 396-399 | 4 | 3 |
| β-strand | 405 | 1 | 4 |
| α-helix | 407-428 | 22 | |
Chain D: 26 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-34 | 10 | |
| α-helix | 40-55 | 16 | |
| α-helix | 60-71 | 12 | |
| α-helix | 96-122 | 27 | |
| α-helix | 127-143 | 17 | |
| α-helix | 147-157 | 11 | |
| α-helix | 164 | 1 | |
| α-helix | 165-170 | 6 | |
| α-helix | 171-181 | 11 | |
| α-helix | 184-200 | 17 | |
| α-helix | 204-220 | 17 | |
| α-helix | 224-234 | 11 | |
| α-helix | 246-260 | 15 | |
| α-helix | 263-266 | 4 | |
| α-helix | 267-271 | 5 | |
| α-helix | 276-279 | 4 | |
| α-helix | 280-282 | 3 | |
| α-helix | 286-297 | 12 | |
| α-helix | 301-311 | 11 | |
| α-helix | 312-316 | 5 | |
| α-helix | 323-325 | 3 | |
| α-helix | 326-342 | 17 | |
| β-strand | 345-349 | 5 | 3 |
| α-helix | 350-357 | 8 | |
| α-helix | 361-371 | 11 | |
| α-helix | 372-374 | 3 | |
| β-strand | 379-382 | 4 | 3 |
| β-strand | 387-390 | 4 | 3 |
| β-strand | 395 | 1 | 4 |
| α-helix | 396-423 | 28 | |
Chain E: 9 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-10 | 3 | 5 |
| α-helix | 12-25 | 14 | |
| β-strand | 34-40 | 7 | 5 |
| β-strand | 46-53 | 8 | 5 |
| β-strand | 56-58 | 3 | 6 |
| β-strand | 66-68 | 3 | 6 |
| α-helix | 70-81 | 12 | |
| β-strand | 88-94 | 7 | 5 |
| α-helix | 103-110 | 8 | |
| β-strand | 120-123 | 4 | 5 |
| β-strand | 134-140 | 7 | 5 |
| β-strand | 153-157 | 5 | 5 |
| β-strand | 161 | 1 | 5 |
| α-helix | 165-175 | 11 | |
| α-helix | 186-215 | 30 | |
| α-helix | 219-221 | 3 | |
| α-helix | 223-234 | 12 | |
| α-helix | 237-238 | 2 | |
| α-helix | 261-306 | 46 | |
Chain F: 26 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-16 | 10 | |
| α-helix | 20-22 | 3 | |
| α-helix | 24-35 | 12 | |
| α-helix | 38-51 | 14 | |
| α-helix | 52-54 | 3 | |
| α-helix | 58-61 | 4 | |
| α-helix | 62-66 | 5 | |
| α-helix | 67-68 | 2 | |
| α-helix | 69-71 | 3 | |
| α-helix | 75-88 | 14 | |
| α-helix | 92-112 | 21 | |
| α-helix | 122-140 | 19 | |
| α-helix | 143-159 | 17 | |
| α-helix | 165-182 | 18 | |
| α-helix | 185-198 | 14 | |
| α-helix | 207-223 | 17 | |
| α-helix | 231-234 | 4 | |
| α-helix | 239-242 | 4 | |
| α-helix | 246-248 | 3 | |
| α-helix | 249-259 | 11 | |
| α-helix | 263-276 | 14 | |
| α-helix | 278-281 | 4 | |
| α-helix | 284-302 | 19 | |
| β-strand | 308-309 | 2 | 2 |
| α-helix | 310-317 | 8 | |
| α-helix | 324-333 | 10 | |
| β-strand | 337-338 | 2 | 7 |
| β-strand | 341-342 | 2 | 2 |
| β-strand | 347-348 | 2 | 2 |
| β-strand | 352-353 | 2 | 7 |
| α-helix | 360-384 | 25 | |
Chain G: 10 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-29 | 4 | 8 |
| α-helix | 31-44 | 14 | |
| β-strand | 50-56 | 7 | 8 |
| β-strand | 62-71 | 10 | 8 |
| α-helix | 85-96 | 12 | |
| β-strand | 103-108 | 6 | 8 |
| β-strand | 110 | 1 | 8 |
| α-helix | 120-128 | 9 | |
| β-strand | 137-141 | 5 | 8 |
| α-helix | 151-152 | 2 | |
| β-strand | 153-158 | 6 | 8 |
| α-helix | 187-190 | 4 | |
| β-strand | 196-198 | 3 | 8 |
| β-strand | 201-202 | 2 | 8 |
| α-helix | 207-214 | 8 | |
| α-helix | 230-260 | 31 | |
| α-helix | 263-270 | 8 | |
| α-helix | 276-300 | 25 | |
| α-helix | 301-305 | 5 | |
Chain H: 12 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-17 | 10 | |
| α-helix | 20-40 | 21 | |
| α-helix | 52-71 | 20 | |
| α-helix | 75-90 | 16 | |
| α-helix | 101-115 | 15 | |
| α-helix | 119-133 | 15 | |
| α-helix | 143-154 | 12 | |
| α-helix | 157-166 | 10 | |
| α-helix | 175-196 | 22 | |
| β-strand | 199-201 | 3 | 9 |
| α-helix | 202-209 | 8 | |
| α-helix | 215-223 | 9 | |
| β-strand | 228-229 | 2 | 9 |
| β-strand | 232-234 | 3 | 9 |
| α-helix | 259-271 | 13 | |
1 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 |
|---|
| 26S proteasome regulatory subunit RPN3 | A | protein | 438 | Saccharomyces cerevisiae S288c | P40016 (AlphaFold model) |
| 26S proteasome regulatory subunit RPN5 | B | protein | 445 | Saccharomyces cerevisiae S288c | Q12250 (AlphaFold model) |
| 26S proteasome regulatory subunit RPN6 | C | protein | 434 | Saccharomyces cerevisiae S288c | Q12377 (AlphaFold model) |
| 26S proteasome regulatory subunit RPN7 | D | protein | 429 | Saccharomyces cerevisiae S288c | Q06103 (AlphaFold model) |
| 26S proteasome regulatory subunit RPN8 | E | protein | 338 | Saccharomyces cerevisiae S288c | Q08723 |
| 26S proteasome regulatory subunit RPN9 | F | protein | 393 | Saccharomyces cerevisiae S288c | Q04062 |
| Ubiquitin carboxyl-terminal hydrolase RPN11 | G | protein | 306 | Saccharomyces cerevisiae S288c | P43588 |
| 26S proteasome regulatory subunit RPN12 | H | protein | 274 | Saccharomyces cerevisiae S288c | P32496 |
| 26S proteasome complex subunit SEM1 | I | protein | 89 | Saccharomyces cerevisiae S288c | O94742 |
Sequence of entity 1 (A), FASTA
>3JCK_1 26S proteasome regulatory subunit RPN3 (chains A)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXTAEINCFMHLLVQLF
LWDSKELEQLVEFNRKVVIPNLLCYYNLRSLNLINAKLWFYIYLSHETLARSSEEINSDN
QNIILRSTMMKFLKIASLKHDNETKAMLINLILRDFLNNGEVDSASDFISKLEYPHTDVS
SSLEARYFFYLSKINAIQLDYSTANEYIIAAIRKAPHNSKSLGFLQQSNKLHCCIQLLMG
DIPELSFFHQSNMQKSLLPYYHLTKAVKLGDLKKFTSTITKYKQLLLKDDTYQLCVRLRS
NVIKTGIRIISLTYKKISLRDICLKLNLDSEQTVEYMVSRAIRDGVIEAKINHEDGFIET
TELLNIYDSEDPQQVFDERIKFANQLHDEYLVSMRYPEDKKTQQNEKSENGENDDDTLDG
DLMDDMSDISDLDDLGFL
Sequence of entity 2 (B), FASTA
>3JCK_2 26S proteasome regulatory subunit RPN5 (chains B)
MSRDAPIKADKDYSQILKEEFPKIDSLAQNDCNSALDQLLVLEKKTRQASDLASSKEVLA
KIVDLLASRNKWDDLNEQLTLLSKKHGQLKLSIQYMIQKVMEYLKSSKSLDLNTRISVIE
TIRVVTENKIFVEVERARVTKDLVEIKKEEGKIDEAADILCELQVETYGSMEMSEKIQFI
LEQMELSILKGDYSQATVLSRKILKKTFKNPKYESLKLEYYNLLVKISLHKREYLEVAQY
LQEIYQTDAIKSDEAKWKPVLSHIVYFLVLSPYGNLQNDLIHKIQNDNNLKKLESQESLV
KLFTTNELMRWPIVQKTYEPVLNEDDLAFGGEANKHHWEDLQKRVIEHNLRVISEYYSRI
TLLRLNELLDLTESQTETYISDLVNQGIIYAKVNRPAKIVNFEKPKNSSQLLNEWSHNVD
ELLEHIETIGHLITKEEIMHGLQAK
Sequence of entity 3 (C), FASTA
>3JCK_3 26S proteasome regulatory subunit RPN6 (chains C)
MSLPGSKLEEARRLVNEKQYNEAEQVYLSLLDKDSSQSSAAAGASVDDKRRNEQETSILE
LGQLYVTMGAKDKLREFIPHSTEYMMQFAKSKTVKVLKTLIEKFEQVPDSLDDQIFVCEK
SIEFAKREKRVFLKHSLSIKLATLHYQKKQYKDSLALINDLLREFKKLDDKPSLVDVHLL
ESKVYHKLRNLAKSKASLTAARTAANSIYCPTQTVAELDLMSGILHCEDKDYKTAFSYFF
ESFESYHNLTTHNSYEKACQVLKYMLLSKIMLNLIDDVKNILNAKYTKETYQSRGIDAMK
AVAEAYNNRSLLDFNTALKQYEKELMGDELTRSHFNALYDTLLESNLCKIIEPFECVEIS
HISKIIGLDTQQVEGKLSQMILDKIFYGVLDQGNGWLYVYETPNQDATYDSALELVGQLN
KVVDQLFEKASVLY
Sequence of entity 4 (D), FASTA
>3JCK_4 26S proteasome regulatory subunit RPN7 (chains D)
MVDVEEKSQEVEYVDPTVNRVPNYEVSEKAFLLTQSKVSIEQRKEAAEFVLAKIKEEEMA
PYYKYLCEEYLVNNGQSDLEHDEKSDSLNEWIKFDQELYNELCKKNESKIKELNEKIQKL
EEDDEGELEQAQAWINLGEYYAQIGDKDNAEKTLGKSLSKAISTGAKIDVMLTIARLGFF
YNDQLYVKEKLEAVNSMIEKGGDWERRNRYKTYYGIHCLAVRNFKEAAKLLVDSLATFTS
IELTSYESIATYASVTGLFTLERTDLKSKVIDSPELLSLISTTAALQSISSLTISLYASD
YASYFPYLLETYANVLIPCKYLNRHADFFVREMRRKVYAQLLESYKTLSLKSMASAFGVS
VAFLDNDLGKFIPNKQLNCVIDRVNGIVETNRPDNKNAQYHLLVKQGDGLLTKLQKYGAA
VRLTGSDRV
Sequence of entity 5 (E), FASTA
>3JCK_5 26S proteasome regulatory subunit RPN8 (chains E)
MSLQHEKVTIAPLVLLSALDHYERTQTKENKRCVGVILGDANSSTIRVTNSFALPFEEDE
KNSDVWFLDHNYIENMNEMCKKINAKEKLIGWYHSGPKLRASDLKINELFKKYTQNNPLL
LIVDVKQQGVGLPTDAYVAIEQVKDDGTSTEKTFLHLPCTIEAEEAEEIGVEHLLRDVRD
QAAGGLSIRLTNQLKSLKGLQSKLKDVVEYLDKVINKELPINHTILGKLQDVFNLLPNLG
TPDDDEIDVENHDRINISNNLQKALTVKTNDELMVIYISNLVRSIIAFDDLIENKIQNKK
IQEQRVKDKQSKVSDDSESESGDKEATAPLIQRKNKKN
Sequence of entity 6 (F), FASTA
>3JCK_6 26S proteasome regulatory subunit RPN9 (chains F)
MFNNHEIDTILSTLRMEADPSLHPLFEQFEKFYEEKLWFQLSESLTKFFDDAKSTPLRLR
LYDNFVSKFYDKINQLSVVKYLLASLKDSKDFDESLKYLDDLKAQFQELDSKKQRNNGSK
DHGDGILLIDSEIARTYLLKNDLVKARDLLDDLEKTLDKKDSIPLRITNSFYSTNSQYFK
FKNDFNSFYYTSLLYLSTLEPSTSITLAERQQLAYDLSISALLGDKIYNFGELLHHPIME
TIVNDSNYDWLFQLLNALTVGDFDKFDSLIKVQISKIPILAQHESFLRQKICLMTLIETV
FVKNIRMLSFEDISKATHLPKDNVEHLVMRAISLGLLKGSIDQVNELVTISWVQPRIISG
DQITKMKDRLVEWNDQVEKLGKKMEARGQSIWV
Sequence of entity 7 (G), FASTA
>3JCK_7 Ubiquitin carboxyl-terminal hydrolase RPN11 (chains G)
MERLQRLMMNSKVGSADTGRDDTKETVYISSIALLKMLKHGRAGVPMEVMGLMLGEFVDD
YTVNVVDVFAMPQSGTGVSVEAVDDVFQAKMMDMLKQTGRDQMVVGWYHSHPGFGCWLSS
VDVNTQKSFEQLNSRAVAVVVDPIQSVKGKVVIDAFRLIDTGALINNLEPRQTTSNTGLL
NKANIQALIHGLNRHYYSLNIDYHKTAKETKMLMNLHKEQWQSGLKMYDYEEKEESNLAA
TKSMVKIAEQYSKRIEEEKELTEEELKTRYVGRQDPKKHLSETADETLENNIVSVLTAGV
NSVAIK
Sequence of entity 8 (H), FASTA
>3JCK_8 26S proteasome regulatory subunit RPN12 (chains H)
MPSLAELTKSLSIAFENGDYAACEKLLPPIKIELIKNNLLIPDLSIQNDIYLNDLMITKR
ILEVGALASIQTFNFDSFENYFNQLKPYYFSNNHKLSESDKKSKLISLYLLNLLSQNNTT
KFHSELQYLDKHIKNLEDDSLLSYPIKLDRWLMEGSYQKAWDLLQSGSQNISEFDSFTDI
LKSAIRDEIAKNTELSYDFLPLSNIKALLFFNNEKETEKFALERNWPIVNSKVYFNNQSK
EKADYEDEMMHEEDQKTNIIEKAMDYAISIENIV
Sequence of entity 9 (I), FASTA
>3JCK_9 26S proteasome complex subunit SEM1 (chains I)
MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIW
EENWDDVEVDDDFTNELKAELDRYKRENQ
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 1 |
Primary citation
Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition. Dambacher, C.M., Worden, E.J., Herzik, M.A. et al. Elife (2016) 5:e13027-e13027. DOI 10.7554/eLife.13027 · PubMed
Other PDB entries of the same protein (UniProt P40016 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9CGC 3.61 Å, Yeast 26S proteasome non-substrate-engaged (S1 state)
- 6J2Q 3.8 Å, Yeast proteasome in Ub-accepted state (C1-b)
- 6J2X 3.8 Å, Yeast proteasome in resting state (C1-a)
- 5MPD 4.1 Å, 26S proteasome in presence of ATP (s1)
- 6FVT 4.1 Å, 26S proteasome, s1 state
- 5WVK 4.2 Å, Yeast proteasome-ADP-AlFx
- 5MPE 4.5 Å, 26S proteasome in presence of ATP (s2)
- 6FVU 4.5 Å, 26S proteasome, s2 state
- 6FVW 4.5 Å, 26S proteasome, s4 state
- 6J30 4.5 Å, yeast proteasome in Ub-engaged state (C2)
- 3JCP 4.6 Å, Structure of yeast 26S proteasome in M2 state derived from Titan dataset
- 3JCO 4.8 Å, Structure of yeast 26S proteasome in M1 state derived from Titan dataset
Browse structure collections
About this viewer
MolViewer shows 3JCK 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.