9ETZ: Cytochrome b-c1 complex subunit 1, mitochondrial
III2IV respiratory supercomplex from Saccharomyces cerevisiae. Determined by electron microscopy at 2.4 Å resolution. Released 2 Oct 2024.
- Method
- Electron microscopy
- Resolution
- 2.4 Å
- Organism
- Saccharomyces cerevisiae
- Chains
- 32
- Atoms
- 48,795
- Mol. weight
- 701.79 kDa
- Ligands
- HEM, PEF, PCF, UQ6
- Released
- 2 Oct 2024
Explore 9ETZ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9ETZ contains 333 α-helices and 143 β-strands across 32 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: 31 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-5 | 4 | |
| α-helix | 11-39 | 29 | |
| α-helix | 52-66 | 15 | |
| α-helix | 67-71 | 5 | |
| α-helix | 72-75 | 4 | |
| α-helix | 79-88 | 10 | |
| α-helix | 96-117 | 22 | |
| α-helix | 143-171 | 29 | |
| β-strand | 175 | 1 | 41 |
| α-helix | 179-181 | 3 | |
| α-helix | 184-215 | 32 | |
| α-helix | 229-261 | 33 | |
| α-helix | 266-267 | 2 | |
| α-helix | 270-283 | 14 | |
| α-helix | 288-291 | 4 | |
| α-helix | 299-310 | 12 | |
| α-helix | 313-327 | 15 | |
| α-helix | 336-358 | 23 | |
| α-helix | 363-366 | 4 | |
| β-strand | 370 | 1 | 42 |
| α-helix | 371-379 | 9 | |
| α-helix | 381-385 | 5 | |
| α-helix | 386-401 | 16 | |
| α-helix | 407-425 | 19 | |
| α-helix | 428-434 | 7 | |
| α-helix | 436 | 1 | |
| β-strand | 437 | 1 | 42 |
| α-helix | 445-447 | 3 | |
| α-helix | 448-478 | 31 | |
| α-helix | 481-483 | 3 | |
| α-helix | 494-496 | 3 | |
| α-helix | 501-504 | 4 | |
| α-helix | 514-517 | 4 | |
| α-helix | 530-531 | 2 | |
| β-strand | 532-533 | 2 | 41 |
Chain A: 24 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 29-31 | 3 | 1 |
| β-strand | 37-42 | 6 | 1 |
| β-strand | 49-55 | 7 | 1 |
| α-helix | 59-61 | 3 | |
| α-helix | 69-77 | 9 | |
| α-helix | 80-88 | 9 | |
| β-strand | 92-97 | 6 | 1 |
| β-strand | 102-108 | 7 | 1 |
| α-helix | 113-120 | 8 | |
| α-helix | 121-125 | 5 | |
| α-helix | 137-154 | 18 | |
| α-helix | 156-168 | 13 | |
| α-helix | 173-175 | 3 | |
| α-helix | 182-187 | 6 | |
| α-helix | 190-200 | 11 | |
| β-strand | 202 | 1 | 2 |
| α-helix | 203-205 | 3 | |
| β-strand | 206-212 | 7 | 1 |
| α-helix | 216-226 | 11 | |
| β-strand | 231 | 1 | 2 |
| α-helix | 235-238 | 4 | |
| β-strand | 247-253 | 7 | 3 |
| β-strand | 259-266 | 8 | 3 |
| α-helix | 275-285 | 11 | |
| β-strand | 287-289 | 3 | 3 |
| α-helix | 293-296 | 4 | |
| α-helix | 303-306 | 4 | |
| β-strand | 314-321 | 8 | 3 |
| β-strand | 326-334 | 9 | 3 |
| α-helix | 337-339 | 3 | |
| α-helix | 340-356 | 17 | |
| α-helix | 360-378 | 19 | |
| α-helix | 383-397 | 15 | |
| α-helix | 403-411 | 9 | |
| α-helix | 415-425 | 11 | |
| β-strand | 432-437 | 6 | 3 |
| α-helix | 445-449 | 5 | |
| α-helix | 450-452 | 3 | |
Chain b: 10 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-28 | 4 | |
| α-helix | 31-65 | 35 | |
| α-helix | 79-108 | 30 | |
| β-strand | 115-122 | 8 | 43 |
| β-strand | 125-130 | 6 | 43 |
| β-strand | 141-145 | 5 | 43 |
| β-strand | 147 | 1 | 44 |
| α-helix | 148-149 | 2 | |
| α-helix | 150-152 | 3 | |
| α-helix | 153-154 | 2 | |
| α-helix | 157-158 | 2 | |
| β-strand | 163 | 1 | 44 |
| β-strand | 167-170 | 4 | 45 |
| β-strand | 174-181 | 8 | 43 |
| β-strand | 186-190 | 5 | 46 |
| α-helix | 191-193 | 3 | |
| β-strand | 195-199 | 5 | 46 |
| β-strand | 205-210 | 6 | 43 |
| β-strand | 215-219 | 5 | 45 |
| α-helix | 227-230 | 4 | |
| β-strand | 234-239 | 6 | 45 |
| α-helix | 241-250 | 10 | |
Chain B: 21 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 4 |
| β-strand | 28-35 | 8 | 4 |
| α-helix | 39-41 | 3 | |
| α-helix | 47-53 | 7 | |
| β-strand | 59 | 1 | 5 |
| α-helix | 64-72 | 9 | |
| β-strand | 76-82 | 7 | 4 |
| β-strand | 87-94 | 8 | 4 |
| α-helix | 95-97 | 3 | |
| α-helix | 98-108 | 11 | |
| β-strand | 112 | 1 | 5 |
| α-helix | 116-118 | 3 | |
| α-helix | 119-123 | 5 | |
| α-helix | 124-134 | 11 | |
| α-helix | 138-150 | 13 | |
| α-helix | 169-179 | 11 | |
| α-helix | 182-184 | 3 | |
| β-strand | 185-190 | 6 | 4 |
| α-helix | 194-202 | 9 | |
| α-helix | 205-208 | 4 | |
| α-helix | 220-222 | 3 | |
| β-strand | 228-232 | 5 | 6 |
| β-strand | 237-245 | 9 | 6 |
| α-helix | 250-261 | 12 | |
| α-helix | 266-269 | 4 | |
| β-strand | 273-278 | 6 | 6 |
| β-strand | 283-291 | 9 | 6 |
| α-helix | 294-310 | 17 | |
| β-strand | 312-313 | 2 | 7 |
| α-helix | 318-328 | 11 | |
| α-helix | 335-338 | 4 | |
| β-strand | 345-346 | 2 | 7 |
| β-strand | 352-357 | 6 | 6 |
| α-helix | 359-361 | 3 | |
| α-helix | 365-367 | 3 | |
Chain c: 14 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-8 | 3 | |
| α-helix | 17-19 | 3 | |
| α-helix | 22-40 | 19 | |
| α-helix | 49-74 | 26 | |
| α-helix | 81-113 | 33 | |
| α-helix | 118-120 | 3 | |
| α-helix | 126 | 1 | |
| α-helix | 131-133 | 3 | |
| α-helix | 137-146 | 10 | |
| α-helix | 148-160 | 13 | |
| α-helix | 164-190 | 27 | |
| α-helix | 199-231 | 33 | |
| α-helix | 241-262 | 22 | |
| α-helix | 263-267 | 5 | |
Chain C: 25 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-6 | 4 | |
| α-helix | 8-13 | 6 | |
| α-helix | 14-18 | 5 | |
| β-strand | 21-23 | 3 | 8 |
| α-helix | 28-31 | 4 | |
| α-helix | 32-51 | 20 | |
| α-helix | 61-70 | 10 | |
| α-helix | 75-102 | 28 | |
| α-helix | 108-110 | 3 | |
| α-helix | 111-133 | 23 | |
| β-strand | 137 | 1 | 9 |
| α-helix | 138-147 | 10 | |
| α-helix | 148-153 | 6 | |
| α-helix | 158-166 | 9 | |
| α-helix | 173-201 | 29 | |
| β-strand | 218-220 | 3 | 8 |
| α-helix | 225-245 | 21 | |
| α-helix | 254-257 | 4 | |
| β-strand | 259 | 1 | 9 |
| α-helix | 260 | 1 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-284 | 9 | |
| α-helix | 288-300 | 13 | |
| α-helix | 301-304 | 4 | |
| α-helix | 305-308 | 4 | |
| α-helix | 320-339 | 20 | |
| α-helix | 346-361 | 16 | |
| α-helix | 362-366 | 5 | |
| α-helix | 367-380 | 14 | |
Chain d: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 37-39 | 3 | |
| α-helix | 49-52 | 4 | |
| α-helix | 56-58 | 3 | |
| α-helix | 59-62 | 4 | |
| α-helix | 65-76 | 12 | |
| β-strand | 98-102 | 5 | 47 |
| β-strand | 106 | 1 | 48 |
| β-strand | 109-111 | 3 | 41 |
| β-strand | 122-124 | 3 | 41 |
| β-strand | 127 | 1 | 48 |
| β-strand | 130 | 1 | 48 |
| β-strand | 132-133 | 2 | 47 |
| β-strand | 140-145 | 6 | 47 |
Chain D: 15 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 64-67 | 4 | |
| α-helix | 69-71 | 3 | |
| α-helix | 87-99 | 13 | |
| α-helix | 101-103 | 3 | |
| β-strand | 111 | 1 | 10 |
| α-helix | 112-115 | 4 | |
| β-strand | 116 | 1 | 11 |
| β-strand | 120 | 1 | 11 |
| α-helix | 122-129 | 8 | |
| β-strand | 133-135 | 3 | 12 |
| β-strand | 146-148 | 3 | 12 |
| β-strand | 154 | 1 | 10 |
| α-helix | 155-157 | 3 | |
| α-helix | 162-168 | 7 | |
| α-helix | 174-176 | 3 | |
| α-helix | 188-195 | 8 | |
| α-helix | 202-203 | 2 | |
| β-strand | 213-214 | 2 | 13 |
| β-strand | 222-223 | 2 | 13 |
| α-helix | 244-259 | 16 | |
| α-helix | 263-291 | 29 | |
| α-helix | 293-296 | 4 | |
| β-strand | 298-302 | 5 | 3 |
| α-helix | 304-307 | 4 | |
24 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 |
|---|
| Cytochrome b-c1 complex subunit 1, mitochondrial | A, L | protein | 431 | Saccharomyces cerevisiae | P07256 (AlphaFold model) |
| Cytochrome b-c1 complex subunit 2, mitochondrial | B, M | protein | 352 | Saccharomyces cerevisiae | P07257 (AlphaFold model) |
| Cytochrome b | C, N | protein | 385 | Saccharomyces cerevisiae | P00163 (AlphaFold model) |
| Cytochrome c1, heme protein, mitochondrial | D, O | protein | 247 | Saccharomyces cerevisiae | P07143 (AlphaFold model) |
| Cytochrome b-c1 complex subunit Rieske, mitochondrial | E, P | protein | 185 | Saccharomyces cerevisiae | P08067 |
| Cytochrome b-c1 complex subunit 6, mitochondrial | F, Q | protein | 75 | Saccharomyces cerevisiae | P00127 |
| Cytochrome b-c1 complex subunit 7, mitochondrial | G, R | protein | 126 | Saccharomyces cerevisiae | P00128 |
| Cytochrome b-c1 complex subunit 8, mitochondrial | H, S | protein | 93 | Saccharomyces cerevisiae | P08525 |
| Cytochrome b-c1 complex subunit 9, mitochondrial | I, T | protein | 57 | Saccharomyces cerevisiae | P22289 |
| Cytochrome b-c1 complex subunit 10, mitochondrial | J, U | protein | 76 | Saccharomyces cerevisiae | P37299 |
| Cytochrome c oxidase subunit 1 | a | protein | 534 | Saccharomyces cerevisiae | P00401 |
| Cytochrome c oxidase subunit 2 | b | protein | 236 | Saccharomyces cerevisiae | P00410 |
10 more molecules are not listed.
Sequence of entity 1 (A, L), FASTA
>9ETZ_1 Cytochrome b-c1 complex subunit 1, mitochondrial (chains A, L)
AEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVA
AKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLK
QVQDFEENDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNA
VVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVE
GEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSG
LWGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVND
ANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYM
RIRSDMSMMRW
Sequence of entity 2 (B, M), FASTA
>9ETZ_2 Cytochrome b-c1 complex subunit 2, mitochondrial (chains B, M)
LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGG
TFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ
CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEAD
LKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL
ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSP
AINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL
Sequence of entity 3 (C, N), FASTA
>9ETZ_3 Cytochrome b (chains C, N)
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIEL
AFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII
FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFF
ALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL
ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAIL
VLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF
AYFLIIVPVISTIENVLFYIGRVNK
Sequence of entity 4 (D, O), FASTA
>9ETZ_4 Cytochrome c1, heme protein, mitochondrial (chains D, O)
MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHT
NEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV
KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTP
ATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV
FNPPKPR
Sequence of entity 5 (E, P), FASTA
>9ETZ_5 Cytochrome b-c1 complex subunit Rieske, mitochondrial (chains E, P)
KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLA
MAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP
QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGD
KVIVG
Sequence of entity 6 (F, Q), FASTA
>9ETZ_6 Cytochrome b-c1 complex subunit 6, mitochondrial (chains F, Q)
EVTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQH
YLDTATAPRLFDKLK
Sequence of entity 7 (G, R), FASTA
>9ETZ_7 Cytochrome b-c1 complex subunit 7, mitochondrial (chains G, R)
PQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALR
RLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELD
NIEVSK
Sequence of entity 8 (H, S), FASTA
>9ETZ_8 Cytochrome b-c1 complex subunit 8, mitochondrial (chains H, S)
GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVLI
PAGIYWYWWKNGNEYNEFLYSKAGREELERVNV
Sequence of entity 9 (I, T), FASTA
>9ETZ_9 Cytochrome b-c1 complex subunit 9, mitochondrial (chains I, T)
SFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKARIAA
Sequence of entity 10 (J, U), FASTA
>9ETZ_10 Cytochrome b-c1 complex subunit 10, mitochondrial (chains J, U)
AYTSHLSSKTGLHFGRLSLRSLTAYAPNLMLWGGASMLGLFVFTEGWPKFQDTLYKKIPL
LGPTLEDHTPPEDKPN
Sequence of entity 11 (a), FASTA
>9ETZ_11 Cytochrome c oxidase subunit 1 (chains a)
MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVV
GHAVLMIFFLVMPALIGGFGNYLLPLMIGATDTAFPRINNIAFWVLPMGLVCLVTSTLVE
SGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTLNMRTNGMTMH
KLPLFVWSIFITAFLLLLSLPVLSAGITMLLLDRNFNTSFFEVSGGGDPILYEHLFWFFG
HPEVYILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGFLVWSHHMYIVGLDAD
TRAYFTSATMIIAIPTGIKIFSWLATIHGGSIRLATPMLYAIAFLFLFTMGGLTGVALAN
ASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLNYNEKLAQIQFWLIFIG
ANVIFFPMHFLGINGMPRRIPDYPDAFAGWNYVASIGSFIATLSLFLFIYILYDQLVNGL
NNKVNNKSVIYNKAPDFVESNTIFNLNTVKSSSIEFLLTSPPAVHSFNTPAVQS
Sequence of entity 12 (b), FASTA
>9ETZ_12 Cytochrome c oxidase subunit 2 (chains b)
DVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYTIVMTYSKNPIAYKYI
KHGQTIEVIWTIFPAVILLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFIN
DSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGI
KVDATPGRLNQVSALIQREGVFYGACSELCGTGHANMPIKIEAVSLPKFLEWLNEQ
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 4 |
| PEF | Di-palmitoyl-3-sn-phosphatidylethanolamine | C37 H74 N O8 P | 26 |
| PCF | 1,2-diacyl-sn-glycero-3-phoshocholine | C40 H80 N O8 P | 6 |
| UQ6 | 5-(3,7,11,15,19,23-hexamethyl-tetracosa-2,6,10,14,18,22-hexaenyl)-2,3-dimethoxy… | C39 H60 O4 | 2 |
| HEC | Heme C | C34 H36 Fe N4 O4 | 2 |
| FES | FE2/S2 (inorganic) cluster | Fe2 S2 | 2 |
| CU | Copper (II) ion | Cu | 1 |
| HEA | Heme-a | C49 H56 Fe N4 O6 | 2 |
| CA | Calcium ion | Ca | 1 |
| MG | Magnesium ion | Mg | 1 |
| CUA | Dinuclear copper ion | Cu2 | 1 |
| ZN | Zinc ion | Zn | 1 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 11 |
Primary citation
Electron transfer in the respiratory chain at low salinity. Lobez, A.P., Wu, F., Di Trani, J.M. et al. Nat Commun (2024) 15:8241-8241. DOI 10.1038/s41467-024-52475-3 · PubMed
Other PDB entries of the same protein (UniProt P07256 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3CX5 1.9 Å, Structure of complex III with bound cytochrome c in reduced state and definition of a…
- 1EZV 2.3 Å, Structure of the yeast cytochrome BC1 complex co-crystallized with an antibody fv-fragment
- 1KB9 2.3 Å, Yeast cytochrome BC1 complex
- 2IBZ 2.3 Å, Yeast Cytochrome BC1 Complex with Stigmatellin
- 8YIO 2.35 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in azoxystrobin-bound state
- 8YHQ 2.42 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in pyraclostrobin-bound state
- 1P84 2.5 Å, HDBT inhibited Yeast Cytochrome bc1 Complex
- 3CXH 2.5 Å, Structure of yeast complex III with isoform-2 cytochrome c bound and definition of a…
- 8ZJC 2.5 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex
- 8ZMT 2.52 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in Metyltetraprole-bound state
- 9BPB 2.57 Å, Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae
- 8YIL 2.58 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF24228-bound state
Browse structure collections
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