9BPB: Cytochrome b-c1 complex subunit 1, mitochondrial
Tethered respiratory III2IV2 supercomplex from Saccharomyces cerevisiae. Determined by electron microscopy at 2.57 Å resolution. Released 21 May 2025.
- Method
- Electron microscopy
- Resolution
- 2.57 Å
- Organism
- Saccharomyces cerevisiae W303
- Chains
- 42
- Atoms
- 60,828
- Mol. weight
- 990.98 kDa
- Ligands
- ZN, CUA, MG, CN3
- Released
- 21 May 2025
Explore 9BPB in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9BPB contains 392 α-helices and 174 β-strands across 42 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.
Chains a and m: 27 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-6 | 5 | |
| α-helix | 11-39 | 29 | |
| α-helix | 56-66 | 11 | |
| α-helix | 67-80 | 14 | |
| α-helix | 81-88 | 8 | |
| α-helix | 98-118 | 21 | |
| α-helix | 143-171 | 29 | |
| α-helix | 184-215 | 32 | |
| α-helix | 231-246 | 16 | |
| α-helix | 249-258 | 10 | |
| β-strand | 263 | 1 | 31 |
| α-helix | 270-283 | 14 | |
| α-helix | 284-286 | 3 | |
| α-helix | 289-292 | 4 | |
| α-helix | 299-310 | 12 | |
| α-helix | 313-325 | 13 | |
| β-strand | 332 | 1 | 31 |
| α-helix | 336-358 | 23 | |
| α-helix | 364-366 | 3 | |
| β-strand | 370 | 1 | 32 |
| α-helix | 371-380 | 10 | |
| α-helix | 385-400 | 16 | |
| α-helix | 407-425 | 19 | |
| α-helix | 428-433 | 6 | |
| α-helix | 436 | 1 | |
| β-strand | 437 | 1 | 32 |
| α-helix | 445-447 | 3 | |
| α-helix | 448-476 | 29 | |
| α-helix | 514-517 | 4 | |
| α-helix | 522-523 | 2 | |
| α-helix | 530-531 | 2 | |
| β-strand | 532-533 | 2 | 33 |
Chains A and K: 26 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 29-32 | 4 | 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 | 80-89 | 10 | |
| β-strand | 92-97 | 6 | 1 |
| β-strand | 102-108 | 7 | 1 |
| α-helix | 110-112 | 3 | |
| α-helix | 113-119 | 7 | |
| α-helix | 120-126 | 7 | |
| α-helix | 134-154 | 21 | |
| α-helix | 156-168 | 13 | |
| α-helix | 173-175 | 3 | |
| α-helix | 182-187 | 6 | |
| α-helix | 190-200 | 11 | |
| α-helix | 203-205 | 3 | |
| β-strand | 206-212 | 7 | 1 |
| α-helix | 216-225 | 10 | |
| α-helix | 235-238 | 4 | |
| β-strand | 247-253 | 7 | 2 |
| β-strand | 259-266 | 8 | 2 |
| α-helix | 268-269 | 2 | |
| α-helix | 275-285 | 11 | |
| β-strand | 288-289 | 2 | 2 |
| α-helix | 294-296 | 3 | |
| α-helix | 303-306 | 4 | |
| β-strand | 314-321 | 8 | 2 |
| β-strand | 326-334 | 9 | 2 |
| α-helix | 340-357 | 18 | |
| α-helix | 360-378 | 19 | |
| α-helix | 383-394 | 12 | |
| α-helix | 403-411 | 9 | |
| α-helix | 415-425 | 11 | |
| β-strand | 432-437 | 6 | 2 |
| α-helix | 439-441 | 3 | |
| α-helix | 445-449 | 5 | |
| α-helix | 450-452 | 3 | |
Chains b and n: 8 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-28 | 4 | |
| α-helix | 31-65 | 35 | |
| α-helix | 79-106 | 28 | |
| β-strand | 115-121 | 7 | 34 |
| β-strand | 126-130 | 5 | 34 |
| β-strand | 141-145 | 5 | 34 |
| α-helix | 146 | 1 | |
| β-strand | 147 | 1 | 35 |
| α-helix | 148-149 | 2 | |
| α-helix | 157-158 | 2 | |
| β-strand | 163 | 1 | 35 |
| β-strand | 167-170 | 4 | 36 |
| β-strand | 174-181 | 8 | 34 |
| β-strand | 188-190 | 3 | 37 |
| α-helix | 191-193 | 3 | |
| β-strand | 195-197 | 3 | 37 |
| β-strand | 205-210 | 6 | 34 |
| β-strand | 215-217 | 3 | 36 |
| β-strand | 220-221 | 2 | 37 |
| β-strand | 236-239 | 4 | 36 |
| α-helix | 241-248 | 8 | |
Chains B and L: 19 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 3 |
| β-strand | 28-35 | 8 | 3 |
| α-helix | 39-41 | 3 | |
| α-helix | 47-54 | 8 | |
| β-strand | 59 | 1 | 4 |
| α-helix | 64-73 | 10 | |
| β-strand | 77-82 | 6 | 3 |
| β-strand | 87-94 | 8 | 3 |
| α-helix | 98-108 | 11 | |
| β-strand | 112 | 1 | 4 |
| α-helix | 116-118 | 3 | |
| α-helix | 119-123 | 5 | |
| α-helix | 124-136 | 13 | |
| α-helix | 138-150 | 13 | |
| α-helix | 169-179 | 11 | |
| β-strand | 185-190 | 6 | 3 |
| α-helix | 194-201 | 8 | |
| α-helix | 205-208 | 4 | |
| α-helix | 220-222 | 3 | |
| β-strand | 228-232 | 5 | 5 |
| β-strand | 237-245 | 9 | 5 |
| α-helix | 250-259 | 10 | |
| α-helix | 266-269 | 4 | |
| β-strand | 273-278 | 6 | 5 |
| β-strand | 283-288 | 6 | 5 |
| β-strand | 290-291 | 2 | 5 |
| α-helix | 294-310 | 17 | |
| β-strand | 312-313 | 2 | 6 |
| α-helix | 315-317 | 3 | |
| α-helix | 318-328 | 11 | |
| α-helix | 338-342 | 5 | |
| β-strand | 345-346 | 2 | 6 |
| β-strand | 352-357 | 6 | 5 |
| α-helix | 363-364 | 2 | |
Chains c and o: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-6 | 4 | |
| α-helix | 17-19 | 3 | |
| α-helix | 22-40 | 19 | |
| α-helix | 49-74 | 26 | |
| α-helix | 81-114 | 34 | |
| α-helix | 126 | 1 | |
| α-helix | 131-133 | 3 | |
| α-helix | 138-161 | 24 | |
| α-helix | 164-190 | 27 | |
| α-helix | 199-231 | 33 | |
| α-helix | 241-261 | 21 | |
| α-helix | 262-266 | 5 | |
Chains C and M: 24 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-6 | 4 | |
| α-helix | 10-13 | 4 | |
| α-helix | 14-18 | 5 | |
| β-strand | 21-23 | 3 | 7 |
| α-helix | 28-31 | 4 | |
| α-helix | 32-48 | 17 | |
| α-helix | 51-53 | 3 | |
| α-helix | 61-70 | 10 | |
| α-helix | 75-102 | 28 | |
| α-helix | 111-134 | 24 | |
| β-strand | 137 | 1 | 8 |
| α-helix | 138-148 | 11 | |
| α-helix | 149-153 | 5 | |
| α-helix | 158-166 | 9 | |
| α-helix | 173-201 | 29 | |
| β-strand | 218-220 | 3 | 7 |
| α-helix | 225-245 | 21 | |
| α-helix | 254-257 | 4 | |
| β-strand | 259 | 1 | 8 |
| α-helix | 260 | 1 | |
| α-helix | 276-284 | 9 | |
| α-helix | 289-300 | 12 | |
| α-helix | 301-304 | 4 | |
| α-helix | 305-308 | 4 | |
| β-strand | 313 | 1 | 9 |
| α-helix | 322-339 | 18 | |
| α-helix | 348-361 | 14 | |
| α-helix | 362-366 | 5 | |
| α-helix | 367-380 | 14 | |
Chains d and p: 5 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 43-46 | 4 | |
| α-helix | 49-52 | 4 | |
| α-helix | 66-75 | 10 | |
| α-helix | 84-87 | 4 | |
| β-strand | 93 | 1 | 38 |
| β-strand | 96 | 1 | 38 |
| α-helix | 97 | 1 | |
| β-strand | 98-102 | 5 | 39 |
| β-strand | 106 | 1 | 40 |
| β-strand | 109-111 | 3 | 33 |
| β-strand | 122-124 | 3 | 33 |
| β-strand | 127 | 1 | 40 |
| β-strand | 130 | 1 | 40 |
| β-strand | 131-132 | 2 | 39 |
| β-strand | 141-145 | 5 | 39 |
Chains D and N: 16 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 69-71 | 3 | |
| α-helix | 87-96 | 10 | |
| α-helix | 97-101 | 5 | |
| β-strand | 106 | 1 | 10 |
| β-strand | 111 | 1 | 11 |
| α-helix | 113-115 | 3 | |
| β-strand | 116 | 1 | 12 |
| β-strand | 120 | 1 | 12 |
| α-helix | 122-128 | 7 | |
| β-strand | 133-136 | 4 | 13 |
| α-helix | 137-138 | 2 | |
| β-strand | 145-148 | 4 | 13 |
| β-strand | 154 | 1 | 11 |
| α-helix | 155-157 | 3 | |
| α-helix | 162-168 | 7 | |
| α-helix | 174-175 | 2 | |
| β-strand | 176 | 1 | 10 |
| α-helix | 187-195 | 9 | |
| α-helix | 202-203 | 2 | |
| α-helix | 208-209 | 2 | |
| β-strand | 213-214 | 2 | 14 |
| β-strand | 222-223 | 2 | 14 |
| α-helix | 244-259 | 16 | |
| α-helix | 263-291 | 29 | |
| α-helix | 293-296 | 4 | |
| β-strand | 299-302 | 4 | 2 |
| α-helix | 304-306 | 3 | |
13 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, K | protein | 457 | Saccharomyces cerevisiae W303 | P07256 (AlphaFold model) |
| Cytochrome b-c1 complex subunit 2, mitochondrial | B, L | protein | 368 | Saccharomyces cerevisiae W303 | P07257 (AlphaFold model) |
| Cytochrome b | C, M | protein | 385 | Saccharomyces cerevisiae W303 | P00163 (AlphaFold model) |
| Cytochrome c1, heme protein, mitochondrial | D, N | protein | 309 | Saccharomyces cerevisiae W303 | P07143 (AlphaFold model) |
| Cytochrome b-c1 complex subunit Rieske, mitochondrial | E, O | protein | 215 | Saccharomyces cerevisiae W303 | P08067 |
| Cytochrome b-c1 complex subunit 6, mitochondrial | F, P | protein | 147 | Saccharomyces cerevisiae W303 | P00127 |
| Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial | G, Q | protein | 183 | Saccharomyces cerevisiae W303 | P00128, P04039 |
| Cytochrome b-c1 complex subunit 8, mitochondrial | H, R | protein | 94 | Saccharomyces cerevisiae W303 | P08525 |
| Cytochrome b-c1 complex subunit 9, mitochondrial | I, S | protein | 66 | Saccharomyces cerevisiae W303 | P22289 |
| Cytochrome b-c1 complex subunit 10, mitochondrial | J, T | protein | 77 | Saccharomyces cerevisiae W303 | P37299 |
| Cytochrome c oxidase subunit 1 | a, m | protein | 534 | Saccharomyces cerevisiae W303 | P00401 |
| Cytochrome c oxidase subunit 2 | b, n | protein | 251 | Saccharomyces cerevisiae W303 | P00410 |
9 more molecules are not listed.
Sequence of entity 1 (A, K), FASTA
>9BPB_1 Cytochrome b-c1 complex subunit 1, mitochondrial (chains A, K)
MLRTVTSKTVSNQFKRSLATAVATPKAEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAA
NENPYNNGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFL
NQSFIQQKANLLSSSNFEATKKSVLKQVQDFEENDHPNRVLEHLHSTAFQNTPLSLPTRG
TLESLENLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKK
KAAFLGSEVRLRDDTLPKAWISLAVEGEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGI
KLLDNIQEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHFTLKQWNRLTISVTD
TEVERAKSLLKLQLGQLYESGNPVNDANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKA
WAGKRLWDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW
Sequence of entity 2 (B, L), FASTA
>9BPB_2 Cytochrome b-c1 complex subunit 2, mitochondrial (chains B, L)
MLSAARLQFAQGSVRRLTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTN
TRSALKLVRESELLGGTFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELT
ESVLPAARYDYAVAEQCPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVY
TKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAA
IGIPVNKASLAQYEVLANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSN
IKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVS
NLPYLDEL
Sequence of entity 3 (C, M), FASTA
>9BPB_3 Cytochrome b (chains C, M)
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIEL
AFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII
FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFF
ALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL
ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAIL
VLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF
AYFLIIVPVISTIENVLFYIGRVNK
Sequence of entity 4 (D, N), FASTA
>9BPB_4 Cytochrome c1, heme protein, mitochondrial (chains D, N)
MFSNLSKRWAQRTLSKSFYSTATGAASKSGKLTQKLVTAGVAAAGITASTLLYADSLTAE
AMTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSH
TNEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLI
VKARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGT
PATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKF
VFNPPKPRK
Sequence of entity 5 (E, O), FASTA
>9BPB_5 Cytochrome b-c1 complex subunit Rieske, mitochondrial (chains E, O)
MLGIRSSVKTCFKPMSLTSKRLISQSLLASKSTYRTPNFDDVLKENNDADKGRSYAYFMV
GAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRH
RTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPC
HGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG
Sequence of entity 6 (F, P), FASTA
>9BPB_6 Cytochrome b-c1 complex subunit 6, mitochondrial (chains F, P)
MGMLELVGEYWEQLKITVVPVVAAAEDDDNEQHEEKAAEGEEKEEENGDEDEDEDEDEDD
DDDDDEDEEEEEEVTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHK
EDCVEEFFHLQHYLDTATAPRLFDKLK
Sequence of entity 7 (G, Q), FASTA
>9BPB_7 Cytochrome b-c1 complex subunit 7, mitochondrial,Cytochrome c oxidase subunit 8, mitochondrial (chains G, Q)
MPQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTAL
RRLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDEL
DNIEVSKGGGGSVHFKDGVYENIPFKVKGRKTPYALSHFGFFAIGFAVPFVACYVQLKKS
GAF
Sequence of entity 8 (H, R), FASTA
>9BPB_8 Cytochrome b-c1 complex subunit 8, mitochondrial (chains H, R)
MGPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVL
IPAGIYWYWWKNGNEYNEFLYSKAGREELERVNV
Sequence of entity 9 (I, S), FASTA
>9BPB_9 Cytochrome b-c1 complex subunit 9, mitochondrial (chains I, S)
MSFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKARIAAGD
GDDDDE
Sequence of entity 10 (J, T), FASTA
>9BPB_10 Cytochrome b-c1 complex subunit 10, mitochondrial (chains J, T)
MAYTSHLSSKTGLHFGRLSLRSLTAYAPNLMLWGGASMLGLFVFTEGWPKFQDTLYKKIP
LLGPTLEDHTPPEDKPN
Sequence of entity 11 (a, m), FASTA
>9BPB_11 Cytochrome c oxidase subunit 1 (chains a, m)
MVQRWLYSTNAKDIAVLYFMLAIFSGMAGTAMSLIIRLELAAPGSQYLHGNSQLFNVLVV
GHAVLMIFFLVMPALIGGFGNYLLPLMIGATDTAFPRINNIAFWVLPMGLVCLVTSTLVE
SGAGTGWTVYPPLSSIQAHSGPSVDLAIFALHLTSISSLLGAINFIVTTLNMRTNGMTMH
KLPLFVWSIFITAFLLLLSLPVLSAGITMLLLDRNFNTSFFEVSGGGDPILYEHLFWFFG
HPEVYILIIPGFGIISHVVSTYSKKPVFGEISMVYAMASIGLLGFLVWSHHMYIVGLDAD
TRAYFTSATMIIAIPTGIKIFSWLATIHGGSIRLATPMLYAIAFLFLFTMGGLTGVALAN
ASLDVAFHDTYYVVGHFHYVLSMGAIFSLFAGYYYWSPQILGLNYNEKLAQIQFWLIFIG
ANVIFFPMHFLGINGMPRRIPDYPDAFAGWNYVASIGSFIATLSLFLFIYILYDQLVNGL
NNKVNNKSVIYNKAPDFVESNTIFNLNTVKSSSIEFLLTSPPAVHSFNTPAVQS
Sequence of entity 12 (b, n), FASTA
>9BPB_12 Cytochrome c oxidase subunit 2 (chains b, n)
MLDLLRLQLTTFIMNDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYT
IVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILLYLCDEVISPAMTIKAI
GYQWYWKYEYSDFINDSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVT
AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGACSELCGTGHANMPIKIEAVS
LPKFLEWLNEQ
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 2 |
| CUA | Dinuclear copper ion | Cu2 | 2 |
| MG | Magnesium ion | Mg | 2 |
| CN3 | (2R,5S,11R,14R)-5,8,11-trihydroxy-2-(nonanoyloxy)-5,11-dioxido-16-oxo-14-[(prop… | C36 H68 O17 P2 | 2 |
| CA | Calcium ion | Ca | 2 |
| CU | Copper (II) ion | Cu | 2 |
| HEA | Heme-a | C49 H56 Fe N4 O6 | 4 |
| PTY | Phosphatidylethanolamine | C40 H80 N O8 P | 10 |
| PCF | 1,2-diacyl-sn-glycero-3-phoshocholine | C40 H80 N O8 P | 8 |
| FES | FE2/S2 (inorganic) cluster | Fe2 S2 | 2 |
| HEC | Heme C | C34 H36 Fe N4 O4 | 2 |
| PEF | Di-palmitoyl-3-sn-phosphatidylethanolamine | C37 H74 N O8 P | 6 |
| 9PE | (1R)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(heptanoyloxy)methyl]et… | C30 H60 N O8 P | 2 |
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 4 |
| UQ6 | 5-(3,7,11,15,19,23-hexamethyl-tetracosa-2,6,10,14,18,22-hexaenyl)-2,3-dimethoxy… | C39 H60 O4 | 4 |
| CN5 | (5S,11R)-5,8,11-trihydroxy-5,11-dioxido-17-oxo-4,6,10,12,16-pentaoxa-5,11-dipho… | C26 H52 O13 P2 | 1 |
| 8PE | (2R)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(tetradecanoyloxy)propyl… | C37 H74 N O8 P | 2 |
| 6PH | (1R)-2-(phosphonooxy)-1-[(tridecanoyloxy)methyl]ethyl pentadecanoate | C31 H61 O8 P | 2 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 8 |
Primary citation
Mitochondrial respirasome-like supercomplexes support metabolic flexibility in yeast. Eldeeb, M.H., Cosner, Z., Carlstrom, A. et al. Nat Commun (2026). DOI 10.1038/s41467-026-72228-8 · 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
- 9ETZ 2.4 Å, III2IV respiratory supercomplex from Saccharomyces cerevisiae
- 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
- 8YIL 2.58 Å, Cryo-EM structure of Saccharomyces cerevisiae bc1 complex in YF24228-bound state
Browse structure collections
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