8PW6: C respirasome from murine liver
C respirasome from murine liver. Determined by electron microscopy at 3.3 Å resolution. Released 24 Apr 2024.
- Method
- Electron microscopy
- Resolution
- 3.3 Å
- Organism
- Mus musculus
- Chains
- 79
- Atoms
- 115,652
- Mol. weight
- 1886.75 kDa
- Ligands
- 3PE, CDL, HEM, HEC
- Released
- 24 Apr 2024
Explore 8PW6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8PW6 contains 760 α-helices and 340 β-strands across 79 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 1: 25 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 33-39 | 7 | |
| α-helix | 45-51 | 7 | |
| α-helix | 53-63 | 11 | |
| α-helix | 65 | 1 | |
| β-strand | 66 | 1 | 57 |
| α-helix | 67 | 1 | |
| β-strand | 74 | 1 | 57 |
| α-helix | 75-80 | 6 | |
| β-strand | 92-97 | 6 | 58 |
| α-helix | 106-113 | 8 | |
| α-helix | 115-129 | 15 | |
| β-strand | 133-138 | 6 | 58 |
| α-helix | 143-159 | 17 | |
| β-strand | 174-179 | 6 | 58 |
| α-helix | 189-197 | 9 | |
| α-helix | 203-205 | 3 | |
| α-helix | 209 | 1 | |
| α-helix | 215-217 | 3 | |
| β-strand | 220-224 | 5 | 58 |
| α-helix | 225-237 | 13 | |
| α-helix | 239-244 | 6 | |
| β-strand | 246-247 | 2 | 59 |
| β-strand | 250-251 | 2 | 59 |
| β-strand | 253-260 | 8 | 60 |
| β-strand | 262 | 1 | 61 |
| β-strand | 266-271 | 6 | 60 |
| β-strand | 275 | 1 | 62 |
| α-helix | 276-279 | 4 | |
| α-helix | 280-284 | 5 | |
| β-strand | 287 | 1 | 61 |
| β-strand | 294-298 | 5 | 60 |
| α-helix | 305-306 | 2 | |
| β-strand | 307-308 | 2 | 60 |
| α-helix | 309-312 | 4 | |
| β-strand | 316 | 1 | 62 |
| α-helix | 319-324 | 6 | |
| β-strand | 333-338 | 6 | 60 |
| α-helix | 343-357 | 15 | |
| α-helix | 363-381 | 19 | |
| α-helix | 387-399 | 13 | |
| α-helix | 407-421 | 15 | |
| α-helix | 423-437 | 15 | |
Chain 2: 12 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-37 | 13 | |
| α-helix | 39 | 1 | |
| β-strand | 40 | 1 | 53 |
| α-helix | 43-46 | 4 | |
| α-helix | 47-58 | 12 | |
| α-helix | 63-73 | 11 | |
| α-helix | 77-86 | 10 | |
| β-strand | 98-103 | 6 | 54 |
| α-helix | 106-110 | 5 | |
| α-helix | 114-124 | 11 | |
| β-strand | 130-131 | 2 | 54 |
| β-strand | 137-142 | 6 | 54 |
| β-strand | 154-156 | 3 | 54 |
| β-strand | 159-162 | 4 | 54 |
| α-helix | 166-178 | 13 | |
| β-strand | 185-186 | 2 | 54 |
| α-helix | 195 | 1 | |
| α-helix | 205-206 | 2 | |
| α-helix | 213-214 | 2 | |
Chain 3: 34 helices, 37 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-13 | 5 | 67 |
| β-strand | 16-20 | 5 | 67 |
| β-strand | 25 | 1 | 68 |
| α-helix | 26-33 | 8 | |
| β-strand | 56-57 | 2 | 69 |
| β-strand | 58-59 | 2 | 67 |
| β-strand | 66-67 | 2 | 69 |
| α-helix | 71 | 1 | |
| β-strand | 72 | 1 | 68 |
| α-helix | 73 | 1 | |
| β-strand | 78-80 | 3 | 67 |
| α-helix | 84-100 | 17 | |
| α-helix | 105-107 | 3 | |
| α-helix | 115-123 | 9 | |
| α-helix | 133-135 | 3 | |
| β-strand | 146-148 | 3 | 70 |
| α-helix | 150-152 | 3 | |
| α-helix | 158-162 | 5 | |
| α-helix | 163-167 | 5 | |
| β-strand | 173-175 | 3 | 71 |
| α-helix | 178-180 | 3 | |
| β-strand | 182-184 | 3 | 71 |
| α-helix | 198-202 | 5 | |
| β-strand | 208-210 | 3 | 70 |
| β-strand | 223-228 | 6 | 72 |
| β-strand | 237-242 | 6 | 72 |
| β-strand | 247-252 | 6 | 72 |
| β-strand | 255 | 1 | 73 |
| β-strand | 260 | 1 | 73 |
| α-helix | 265-269 | 5 | |
| α-helix | 270-275 | 6 | |
| β-strand | 278 | 1 | 74 |
| β-strand | 283-285 | 3 | 75 |
| β-strand | 291-293 | 3 | 75 |
| α-helix | 296-309 | 14 | |
| β-strand | 315-319 | 5 | 75 |
| α-helix | 325-337 | 13 | |
| β-strand | 343-345 | 3 | 75 |
| β-strand | 358 | 1 | 76 |
| α-helix | 359-362 | 4 | |
| β-strand | 364 | 1 | 77 |
| α-helix | 367-373 | 7 | |
| β-strand | 376-380 | 5 | 77 |
| α-helix | 384-387 | 4 | |
| α-helix | 389-401 | 13 | |
| β-strand | 405-409 | 5 | 77 |
| β-strand | 420-423 | 4 | 77 |
| α-helix | 427-434 | 8 | |
| α-helix | 438-445 | 8 | |
| β-strand | 449-454 | 6 | 77 |
| α-helix | 455-458 | 4 | |
| α-helix | 463-481 | 19 | |
| β-strand | 490-493 | 4 | 77 |
| α-helix | 497-505 | 9 | |
| α-helix | 507 | 1 | |
| β-strand | 508-509 | 2 | 75 |
| α-helix | 512-516 | 5 | |
| β-strand | 521-525 | 5 | 75 |
| β-strand | 542-547 | 6 | 75 |
| β-strand | 549 | 1 | 74 |
| β-strand | 559-562 | 4 | 75 |
| β-strand | 571-574 | 4 | 78 |
| β-strand | 580-583 | 4 | 78 |
| α-helix | 584-585 | 2 | |
| α-helix | 596-607 | 12 | |
| α-helix | 616-626 | 11 | |
| β-strand | 633 | 1 | 78 |
| α-helix | 642-651 | 10 | |
| α-helix | 660-661 | 2 | |
| α-helix | 676-680 | 5 | |
| α-helix | 682-692 | 11 | |
Chain 6: 11 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 35-53 | 19 | |
| β-strand | 57 | 1 | 33 |
| β-strand | 58 | 1 | 34 |
| α-helix | 64-73 | 10 | |
| α-helix | 79-82 | 4 | |
| β-strand | 87 | 1 | 34 |
| α-helix | 90-92 | 3 | |
| β-strand | 95-99 | 5 | 33 |
| β-strand | 103 | 1 | 35 |
| α-helix | 107-115 | 9 | |
| β-strand | 122-126 | 5 | 33 |
| α-helix | 127-132 | 6 | |
| α-helix | 134-136 | 3 | |
| β-strand | 142 | 1 | 35 |
| α-helix | 146-148 | 3 | |
| β-strand | 154-156 | 3 | 33 |
| α-helix | 161-162 | 2 | |
| α-helix | 163-179 | 17 | |
| α-helix | 182-188 | 7 | |
Chain 7: 4 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-4 | 2 | 94 |
| β-strand | 10-11 | 2 | 94 |
| α-helix | 23-25 | 3 | |
| α-helix | 40-45 | 6 | |
| α-helix | 48-49 | 2 | |
| β-strand | 50-52 | 3 | 95 |
| β-strand | 56-59 | 4 | 96 |
| α-helix | 64-66 | 3 | |
| β-strand | 71-74 | 4 | 96 |
| β-strand | 82-83 | 2 | 95 |
| β-strand | 90-93 | 4 | 95 |
Chain 9: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2 | 1 | 82 |
| β-strand | 3-4 | 2 | 47 |
| α-helix | 16-28 | 13 | |
| α-helix | 30-43 | 14 | |
| β-strand | 67-69 | 3 | 83 |
| β-strand | 71 | 1 | 84 |
| β-strand | 77 | 1 | 84 |
| α-helix | 84-88 | 5 | |
| β-strand | 94-100 | 7 | 85 |
| β-strand | 106-114 | 9 | 85 |
| α-helix | 123-127 | 5 | |
| β-strand | 133-135 | 3 | 83 |
| β-strand | 143 | 1 | 33 |
| α-helix | 147-149 | 3 | |
| β-strand | 150-151 | 2 | 85 |
| α-helix | 153-162 | 10 | |
| α-helix | 164-174 | 11 | |
Chain A: 22 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-10 | 7 | |
| α-helix | 12-14 | 3 | |
| β-strand | 15-18 | 4 | 1 |
| β-strand | 24-29 | 6 | 1 |
| β-strand | 34-41 | 8 | 1 |
| α-helix | 55-62 | 8 | |
| β-strand | 67 | 1 | 2 |
| α-helix | 74-82 | 9 | |
| β-strand | 85-90 | 6 | 1 |
| β-strand | 95-102 | 8 | 1 |
| α-helix | 103-105 | 3 | |
| α-helix | 106-118 | 13 | |
| β-strand | 120 | 1 | 2 |
| α-helix | 124-143 | 20 | |
| α-helix | 146-157 | 12 | |
| α-helix | 171-176 | 6 | |
| α-helix | 179-189 | 11 | |
| α-helix | 192-194 | 3 | |
| β-strand | 195-201 | 7 | 1 |
| α-helix | 205-215 | 11 | |
| α-helix | 228-230 | 3 | |
| β-strand | 239-244 | 6 | 3 |
| β-strand | 251-258 | 8 | 3 |
| α-helix | 267-277 | 11 | |
| β-strand | 279-281 | 3 | 3 |
| α-helix | 287-289 | 3 | |
| α-helix | 293-301 | 9 | |
| β-strand | 304-314 | 11 | 3 |
| β-strand | 317-326 | 10 | 3 |
| α-helix | 331-348 | 18 | |
| α-helix | 351-368 | 18 | |
| α-helix | 372-385 | 14 | |
| α-helix | 392-401 | 10 | |
| α-helix | 404-414 | 11 | |
| β-strand | 421-426 | 6 | 3 |
| α-helix | 434-440 | 7 | |
Chain a1: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-4 | 3 | |
| α-helix | 6-30 | 25 | |
| α-helix | 35-38 | 4 | |
| α-helix | 42-55 | 14 | |
| α-helix | 66-68 | 3 | |
71 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 | 480 | Mus musculus | Q9CZ13 (AlphaFold model) |
| Cytochrome b-c1 complex subunit 2, mitochondrial | B, M | protein | 453 | Mus musculus | Q9DB77 (AlphaFold model) |
| Cytochrome b | C, N | protein | 381 | Mus musculus | P00158 (AlphaFold model) |
| Cytochrome c1, heme protein, mitochondrial | D, O | protein | 325 | Mus musculus | Q9D0M3 (AlphaFold model) |
| Cytochrome b-c1 complex subunit Rieske, mitochondrial | E, P, T | protein | 274 | Mus musculus | Q9CR68 |
| Cytochrome b-c1 complex subunit 7 | F, Q | protein | 111 | Mus musculus | Q9D855 |
| Cytochrome b-c1 complex subunit 8 | G, R | protein | 82 | Mus musculus | Q9CQ69 |
| Cytochrome b-c1 complex subunit 6, mitochondrial | H, S | protein | 89 | Mus musculus | P99028 |
| Cytochrome b-c1 complex subunit 9 | J, U | protein | 64 | Mus musculus | Q8R1I1 |
| Cytochrome b-c1 complex subunit 10 | K, V | protein | 56 | Mus musculus | Q9CPX8 |
| Cytochrome c oxidase subunit 1 | n | protein | 514 | Mus musculus | P00397 |
| Cytochrome c oxidase subunit 2 | o | protein | 227 | Mus musculus | P00405 |
55 more molecules are not listed.
Sequence of entity 1 (A, L), FASTA
>8PW6_1 Cytochrome b-c1 complex subunit 1, mitochondrial (chains A, L)
MAASAVCRAACSGTQVLLRTRRSPALLRLPALRGTATFAQALQSVPETQVSILDNGLRVA
SEQSSHATCTVGVWIDAGSRYETEKNNGAGYFLEHLAFKGTKNRPGNALEKEVESIGAHL
NAYSTREHTAYLIKALSKDLPKVVELLADIVQNSSLEDSQIEKERDVILREMQENDASMQ
NVVFDYLHATAFQGTPLAQAVEGPSENVRRLSRTDLTDYLNRHYKAPRMVLAAAGGVEHQ
QLLDLAQKHLSSVSRVYEEDAVPGLTPCRFTGSEIRHRDDALPLAHVAIAVEGPGWANPD
NVTLQVANAIIGHYDCTYGGGVHLSSPLASVAVANKLCQSFQTFNISYSDTGLLGAHFVC
DAMSIDDMVFFLQGQWMRLCTSATESEVTRGKNILRNALVSHLDGTTPVCEDIGRSLLTY
GRRIPLAEWESRIQEVDAQMLRDICSKYFYDQCPAVAGYGPIEQLPDYNRIRSGMFWLRF
Sequence of entity 2 (B, M), FASTA
>8PW6_2 Cytochrome b-c1 complex subunit 2, mitochondrial (chains B, M)
MKLLSRAGSFSRFYSLKVAPKVKTSAAPGGVPLQPQDLEFTKLPNGLVIASLENYAPLSR
IGLFVKAGSRYEDSNNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLSVTATRENMA
YTVEGIRSDIEILMEFLLNVTTAPEFRRWEVAALRSQLKIDKAVAFQNSQTRIIENLHDV
AYKNALANPLYCPDYRMGKITSEELHYFVQNHFTSARMALVGLGVSHSVLKQVAEQFLNM
RGGLGLAGAKAKYRGGEIREQNGDNLVHAAIVAESAAIGNAEANAFSVLQHLLGAGPHIK
RGNNTTSLLSQSVAKGSHQPFDVSAFNASYSDSGLFGIYTISQAAAAGEVINAAYNQVKA
VAQGNLSSADVQAAKNKLKAGYLMSVETSEGFLSEIGSQALAAGSYMPPSTVLQQIDSVA
DADVVKAAKKFVSGKKSMAASGNLGHTPFLDEL
Sequence of entity 3 (C, N), FASTA
>8PW6_3 Cytochrome b (chains C, N)
MTNMRKTHPLFKIINHSFIDLPAPSNISSWWNFGSLLGVCLMVQIITGLFLAMHYTSDTM
TAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGLYYGSYTFMETWNIGVLLL
FAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA
FHFILPFIIAALAIVHLLFLHETGSNNPTGLNSDADKIPFHPYYTIKDILGILIMFLILM
TLVLFFPDMLGDPDNYMPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILI
LALMPFLHTSKQRSLMFRPITQILYWILVANLLILTWIGGQPVEHPFIIIGQLASISYFS
IILILMPISGIIEDKMLKLYP
Sequence of entity 4 (D, O), FASTA
>8PW6_4 Cytochrome c1, heme protein, mitochondrial (chains D, O)
MAAAAASLRRTVLGPRGVGLPGASAPGLLGGARSRQLPLRTPQAVSLSSKSGPSRGRKVM
LSALGMLAAGGAGLAVALHSAVSASDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQV
CSSCHSMDYVAYRHLVGVCYTEEEAKALAEEVEVQDGPNDDGEMFMRPGKLSDYFPKPYP
NPEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQ
AIGMAPPIYTEVLEYDDGTPATMSQVAKDVATFLRWASEPEHDHRKRMGLKMLLMMGLLL
PLTYAMKRHKWSVLKSRKLAYRPPK
Sequence of entity 5 (E, P, T), FASTA
>8PW6_5 Cytochrome b-c1 complex subunit Rieske, mitochondrial (chains E, P, T)
MLSVAARSGPFAPVLSATSRGVAGALRPLLQGAVPAASEPPVLDVKRPFLCRESLSGQAA
ARPLVATVGLNVPASVRFSHTDVKVPDFSDYRRAEVLDSTKSSKESSEARKGFSYLVTAT
TTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRT
KKEIDQEAAVEVSQLRDPQHDLDRVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHG
SHYDASGRIRKGPAPLNLEVPAYEFTSDDVVVVG
Sequence of entity 6 (F, Q), FASTA
>8PW6_6 Cytochrome b-c1 complex subunit 7 (chains F, Q)
MAGRSAVSASSKWLDGFRKWYYNAAGFNKLGLMRDDTLHETEDVKEAIRRLPEDLYNDRM
FRIKRALDLTMRHQILPKDQWTKYEEDKFYLEPYLKEVIRERKEREEWAKK
Sequence of entity 7 (G, R), FASTA
>8PW6_7 Cytochrome b-c1 complex subunit 8 (chains G, R)
MGREFGNLARIRHVISYSLSPFEQRAFPSYFSKGIPNVLRRTRERILRVAPPFVVVYLIY
TWGNQEFEQSKRKNPAMYENDK
Sequence of entity 8 (H, S), FASTA
>8PW6_8 Cytochrome b-c1 complex subunit 6, mitochondrial (chains H, S)
MGLEDERKMLTGSGDPKEEEEEELVDPLTTVREHCEQLEKCVKARERLELCDNRVSSRSQ
TEEDCTEELFDFLHARDHCVAHKLFKNLK
Sequence of entity 9 (J, U), FASTA
>8PW6_9 Cytochrome b-c1 complex subunit 9 (chains J, U)
MSSPTIPSRLYSLLFRRTSTFALTIAVGALFFERAFDQGADAIYEHINEGKLWKHIKHKY
ENKE
Sequence of entity 10 (K, V), FASTA
>8PW6_10 Cytochrome b-c1 complex subunit 10 (chains K, V)
MLSRFLGPRYRELARNWIPTAGMWGTVGAVGLVWATDWRLILDWVPYINGKFKKDD
Sequence of entity 11 (n), FASTA
>8PW6_11 Cytochrome c oxidase subunit 1 (chains n)
MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVIVTA
HAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEA
GAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQ
TPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH
PEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVD
TRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLSN
SSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFSGFTLDDTWAKAHFAIMFVG
VNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVLIMIFMIWEAFASKR
EVMSVSYASTNLEWLHGCPPPYHTFEEPTYVKVK
Sequence of entity 12 (o), FASTA
>8PW6_12 Cytochrome c oxidase subunit 2 (chains o)
MAYPFQLGLQDATSPIMEELMNFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQE
VETIWTILPAVILIMIALPSLRILYMMDEINNPVLTVKTMGHQWYWSYEYTDYEDLCFDS
YMIPTNDLKPGELRLLEVDNRVVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLN
QATVTSNRPGLFYGQCSEICGSNHSFMPIVLEMVPLKYFENWSASMI
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| 3PE | 1,2-Distearoyl-sn-glycerophosphoethanolamine | C41 H82 N O8 P | 33 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 16 |
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 4 |
| HEC | Heme C | C34 H36 Fe N4 O4 | 2 |
| FES | FE2/S2 (inorganic) cluster | Fe2 S2 | 4 |
| PC1 | 1,2-diacyl-sn-glycero-3-phosphocholine | C44 H88 N O8 P | 12 |
| CU | Copper (II) ion | Cu | 1 |
| HEA | Heme-a | C49 H56 Fe N4 O6 | 2 |
| MG | Magnesium ion | Mg | 2 |
| CUA | Dinuclear copper ion | Cu2 | 1 |
| ZN | Zinc ion | Zn | 2 |
| TGL | Tristearoylglycerol | C57 H110 O6 | 1 |
| SF4 | Iron/sulfur cluster | Fe4 S4 | 6 |
| FMN | Flavin mononucleotide | C17 H21 N4 O9 P | 1 |
| NDP | NADPH dihydro-nicotinamide-adenine-dinucleotide phosphate | C21 H30 N7 O17 P3 | 1 |
| ZMP | S-[2-({N-[(2S)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}ami… | C25 H49 N2 O8 P S | 2 |
| DGT | 2'-deoxyguanosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
Water and common crystallization additives (NA, K) are not listed.
Primary citation
SCAF1 drives the compositional diversity of mammalian respirasomes. Vercellino, I., Sazanov, L.A. Nat Struct Mol Biol (2024) 31:1061-1071. DOI 10.1038/s41594-024-01255-0 · PubMed
Other PDB entries of the same protein (UniProt Q9CZ13 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7O3H 2.6 Å, Murine CIII2 focus-refined from supercomplex CICIII2
- 7O37 3.2 Å, Murine supercomplex CIII2CIV in the assembled locked conformation
- 7O3C 3.3 Å, Murine supercomplex CIII2CIV in the mature unlocked conformation
- 8IAR 3.4 Å, Respiratory complex CIII2, focus-refined of type I, Wild type mouse under thermoneutral…
- 8IB7 3.4 Å, Respiratory complex CIII2, focus-refined of type IA, Wild type mouse under cold…
- 8PW7 3.5 Å, A respirasome from murine liver
- 7O3E 3.6 Å, Murine supercomplex CIII2CIV in the intermediate locked conformation
- 8IBC 3.6 Å, Respiratory complex CIII2, focus-refined of type IB, Wild type mouse under cold…
- 8PW5 3.6 Å, CS respirasome from murine liver
- 8UCA 3.7 Å, Formation of I2+III2 supercomplex rescues respiratory chain defects
- 8IBG 3.8 Å, Respiratory complex CIII2, focus-refined of type II, Wild type mouse under cold…
- 8IC5 4.1 Å, Respiratory complex CIII2, focus-refined of type I, PERK -/- mouse under cold temperature
Browse structure collections
About this viewer
MolViewer shows 8PW6 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.