7O3E: Cytochrome b-c1 complex subunit 1, mitochondrial
Murine supercomplex CIII2CIV in the intermediate locked conformation. Determined by electron microscopy at 3.6 Å resolution. Released 13 Oct 2021.
- Method
- Electron microscopy
- Resolution
- 3.6 Å
- Organism
- Mus musculus
- Chains
- 31
- Atoms
- 44,039
- Mol. weight
- 676.81 kDa
- Ligands
- TGL, ZN, CUA, MG
- Released
- 13 Oct 2021
Explore 7O3E in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7O3E contains 257 α-helices and 127 β-strands across 31 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: 25 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2 | 1 | |
| α-helix | 3-7 | 5 | |
| α-helix | 12-40 | 29 | |
| α-helix | 51-65 | 15 | |
| α-helix | 66-78 | 13 | |
| α-helix | 79-86 | 8 | |
| α-helix | 95-117 | 23 | |
| α-helix | 142-169 | 28 | |
| α-helix | 178-180 | 3 | |
| α-helix | 183-214 | 32 | |
| α-helix | 228-261 | 34 | |
| α-helix | 270-283 | 14 | |
| α-helix | 288-291 | 4 | |
| α-helix | 299-325 | 27 | |
| α-helix | 336-359 | 24 | |
| α-helix | 361-366 | 6 | |
| β-strand | 370 | 1 | 29 |
| α-helix | 371-378 | 8 | |
| α-helix | 379-385 | 7 | |
| α-helix | 386-401 | 16 | |
| α-helix | 407-425 | 19 | |
| α-helix | 427-434 | 8 | |
| α-helix | 436 | 1 | |
| β-strand | 437 | 1 | 29 |
| α-helix | 445-447 | 3 | |
| α-helix | 448-478 | 31 | |
| α-helix | 492-494 | 3 | |
| β-strand | 510 | 1 | 30 |
Chain A: 22 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-8 | 4 | |
| 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 | 55-61 | 7 | |
| β-strand | 67 | 1 | 2 |
| α-helix | 74-79 | 6 | |
| β-strand | 85-90 | 6 | 1 |
| β-strand | 95-102 | 8 | 1 |
| α-helix | 106-118 | 13 | |
| β-strand | 120 | 1 | 2 |
| α-helix | 125-142 | 18 | |
| α-helix | 145-157 | 13 | |
| 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 | 233-236 | 4 | |
| β-strand | 239-244 | 6 | 3 |
| β-strand | 251-258 | 8 | 3 |
| α-helix | 266-277 | 12 | |
| β-strand | 280-281 | 2 | 3 |
| α-helix | 293-300 | 8 | |
| β-strand | 304-314 | 11 | 3 |
| β-strand | 317-326 | 10 | 3 |
| α-helix | 328-330 | 3 | |
| α-helix | 331-347 | 17 | |
| α-helix | 352-368 | 17 | |
| α-helix | 373-381 | 9 | |
| α-helix | 382-386 | 5 | |
| α-helix | 392-400 | 9 | |
| α-helix | 404-414 | 11 | |
| β-strand | 421-426 | 6 | 3 |
| α-helix | 434-440 | 7 | |
Chain b: 6 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-12 | 4 | |
| α-helix | 15-44 | 30 | |
| α-helix | 62-85 | 24 | |
| β-strand | 95-102 | 8 | 31 |
| β-strand | 105-110 | 6 | 31 |
| β-strand | 116-120 | 5 | 31 |
| β-strand | 122 | 1 | 32 |
| α-helix | 123-124 | 2 | |
| α-helix | 128-129 | 2 | |
| β-strand | 138 | 1 | 32 |
| β-strand | 142-145 | 4 | 33 |
| β-strand | 150-156 | 7 | 31 |
| β-strand | 161-165 | 5 | 34 |
| β-strand | 170-174 | 5 | 34 |
| β-strand | 176 | 1 | 31 |
| β-strand | 180-184 | 5 | 31 |
| β-strand | 190-195 | 6 | 33 |
| β-strand | 208-214 | 7 | 33 |
| α-helix | 216-226 | 11 | |
Chain B: 19 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 25-28 | 4 | 4 |
| β-strand | 34-38 | 5 | 4 |
| β-strand | 44-51 | 8 | 4 |
| α-helix | 55-57 | 3 | |
| α-helix | 60-62 | 3 | |
| α-helix | 65-71 | 7 | |
| α-helix | 72-74 | 3 | |
| β-strand | 77 | 1 | 5 |
| β-strand | 80 | 1 | 5 |
| α-helix | 82-92 | 11 | |
| β-strand | 95-100 | 6 | 4 |
| β-strand | 105-112 | 8 | 4 |
| α-helix | 113-115 | 3 | |
| α-helix | 116-128 | 13 | |
| α-helix | 134-151 | 18 | |
| α-helix | 155-167 | 13 | |
| β-strand | 168-170 | 3 | 6 |
| α-helix | 188-198 | 11 | |
| α-helix | 201-203 | 3 | |
| β-strand | 204-209 | 6 | 4 |
| α-helix | 213-223 | 11 | |
| β-strand | 238-239 | 2 | 6 |
| β-strand | 242-247 | 6 | 7 |
| β-strand | 253-261 | 9 | 7 |
| α-helix | 267-279 | 13 | |
| β-strand | 285 | 1 | 1 |
| α-helix | 294-302 | 9 | |
| β-strand | 308-315 | 8 | 7 |
| β-strand | 320-328 | 9 | 7 |
| α-helix | 333-348 | 16 | |
| α-helix | 354-371 | 18 | |
| α-helix | 375-388 | 14 | |
| α-helix | 395-402 | 8 | |
| α-helix | 407-418 | 12 | |
| β-strand | 422-428 | 7 | 7 |
Chain c: 11 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-13 | 6 | |
| α-helix | 16-37 | 22 | |
| α-helix | 41-62 | 22 | |
| α-helix | 63-68 | 6 | |
| α-helix | 73-106 | 34 | |
| α-helix | 118 | 1 | |
| α-helix | 130-153 | 24 | |
| β-strand | 155 | 1 | 35 |
| α-helix | 157-182 | 26 | |
| α-helix | 191-222 | 32 | |
| α-helix | 233-252 | 20 | |
| α-helix | 253-258 | 6 | |
Chain C: 20 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-14 | 6 | |
| α-helix | 15-19 | 5 | |
| β-strand | 22-24 | 3 | 8 |
| α-helix | 29-32 | 4 | |
| α-helix | 33-51 | 19 | |
| α-helix | 59-71 | 13 | |
| α-helix | 76-103 | 28 | |
| α-helix | 106-108 | 3 | |
| α-helix | 110-132 | 23 | |
| β-strand | 136 | 1 | 9 |
| α-helix | 137-151 | 15 | |
| α-helix | 157-165 | 9 | |
| α-helix | 172-201 | 30 | |
| α-helix | 205-207 | 3 | |
| β-strand | 217-219 | 3 | 8 |
| α-helix | 223-244 | 22 | |
| α-helix | 253-256 | 4 | |
| β-strand | 258 | 1 | 9 |
| α-helix | 272-281 | 10 | |
| α-helix | 287-303 | 17 | |
| α-helix | 304-306 | 3 | |
| α-helix | 319-338 | 20 | |
| α-helix | 347-363 | 17 | |
| α-helix | 365-375 | 11 | |
Chain d: 10 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 19 | 1 | 36 |
| β-strand | 22 | 1 | 36 |
| α-helix | 35-43 | 9 | |
| α-helix | 48-50 | 3 | |
| α-helix | 53-63 | 11 | |
| α-helix | 68-71 | 4 | |
| α-helix | 77-98 | 22 | |
| α-helix | 99-103 | 5 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-111 | 3 | |
| α-helix | 113-125 | 13 | |
| α-helix | 135-137 | 3 | |
| β-strand | 138 | 1 | 37 |
| β-strand | 145 | 1 | 37 |
Chain D: 10 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 6-10 | 5 | |
| α-helix | 23-35 | 13 | |
| α-helix | 37-39 | 3 | |
| β-strand | 42 | 1 | 10 |
| β-strand | 47 | 1 | 11 |
| α-helix | 48-50 | 3 | |
| β-strand | 52 | 1 | 12 |
| β-strand | 56 | 1 | 12 |
| α-helix | 58-68 | 11 | |
| β-strand | 90 | 1 | 11 |
| α-helix | 91-93 | 3 | |
| α-helix | 98-104 | 7 | |
| β-strand | 112 | 1 | 10 |
| α-helix | 124-132 | 9 | |
| β-strand | 148 | 1 | 13 |
| β-strand | 158 | 1 | 13 |
| α-helix | 179-194 | 16 | |
| α-helix | 198-231 | 34 | |
| β-strand | 234-237 | 4 | 3 |
23 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 | 446 | Mus musculus | Q9CZ13 (AlphaFold model) |
| Cytochrome b-c1 complex subunit 2, mitochondrial | B, M | protein | 439 | Mus musculus | Q9DB77 (AlphaFold model) |
| Cytochrome b | C, N | protein | 381 | Mus musculus | P00158 (AlphaFold model) |
| Cytochrome c1, heme protein, mitochondrial | D, O | protein | 241 | Mus musculus | Q9D0M3 (AlphaFold model) |
| Cytochrome b-c1 complex subunit 7 | F, Q | protein | 110 | Mus musculus | Q9D855 |
| Cytochrome b-c1 complex subunit 8 | G, R | protein | 81 | Mus musculus | Q9CQ69 |
| Cytochrome b-c1 complex subunit 6, mitochondrial | H, S | protein | 76 | Mus musculus | P99028 |
| Cytochrome b-c1 complex subunit Rieske, mitochondrial | P | protein | 196 | Mus musculus | Q9CR68 |
| Cytochrome b-c1 complex subunit 9 | T | protein | 78 | Mus musculus | Q9CR68 |
| Cox7a2l protein | I | protein | 113 | Mus musculus | Q99KD6 |
| Cytochrome c oxidase subunit 1 | a | protein | 514 | Mus musculus | P00397 |
| Cytochrome c oxidase subunit 2 | b | protein | 227 | Mus musculus | P00405 |
11 more molecules are not listed.
Sequence of entity 1 (A, L), FASTA
>7O3E_1 Cytochrome b-c1 complex subunit 1, mitochondrial (chains A, L)
TATFAQALQSVPETQVSILDNGLRVASEQSSHATCTVGVWIDAGSRYETEKNNGAGYFLE
HLAFKGTKNRPGNALEKEVESIGAHLNAYSTREHTAYLIKALSKDLPKVVELLADIVQNS
SLEDSQIEKERDVILREMQENDASMQNVVFDYLHATAFQGTPLAQAVEGPSENVRRLSRT
DLTDYLNRHYKAPRMVLAAAGGVEHQQLLDLAQKHLSSVSRVYEEDAVPGLTPCRFTGSE
IRHRDDALPLAHVAIAVEGPGWANPDNVTLQVANAIIGHYDCTYGGGVHLSSPLASVAVA
NKLCQSFQTFNISYSDTGLLGAHFVCDAMSIDDMVFFLQGQWMRLCTSATESEVTRGKNI
LRNALVSHLDGTTPVCEDIGRSLLTYGRRIPLAEWESRIQEVDAQMLRDICSKYFYDQCP
AVAGYGPIEQLPDYNRIRSGMFWLRF
Sequence of entity 2 (B, M), FASTA
>7O3E_2 Cytochrome b-c1 complex subunit 2, mitochondrial (chains B, M)
SLKVAPKVKTSAAPGGVPLQPQDLEFTKLPNGLVIASLENYAPLSRIGLFVKAGSRYEDS
NNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLSVTATRENMAYTVEGIRSDIEILM
EFLLNVTTAPEFRRWEVAALRSQLKIDKAVAFQNSQTRIIENLHDVAYKNALANPLYCPD
YRMGKITSEELHYFVQNHFTSARMALVGLGVSHSVLKQVAEQFLNMRGGLGLAGAKAKYR
GGEIREQNGDNLVHAAIVAESAAIGNAEANAFSVLQHLLGAGPHIKRGNNTTSLLSQSVA
KGSHQPFDVSAFNASYSDSGLFGIYTISQAAAAGEVINAAYNQVKAVAQGNLSSADVQAA
KNKLKAGYLMSVETSEGFLSEIGSQALAAGSYMPPSTVLQQIDSVADADVVKAAKKFVSG
KKSMAASGNLGHTPFLDEL
Sequence of entity 3 (C, N), FASTA
>7O3E_3 Cytochrome b (chains C, N)
MTNMRKTHPLFKIINHSFIDLPAPSNISSWWNFGSLLGVCLMVQIITGLFLAMHYTSDTM
TAFSSVTHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGLYYGSYTFMETWNIGVLLL
FAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFA
FHFILPFIIAALAIVHLLFLHETGSNNPTGLNSDADKIPFHPYYTIKDILGILIMFLILM
TLVLFFPDMLGDPDNYMPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILI
LALMPFLHTSKQRSLMFRPITQILYWILVANLLILTWIGGQPVEHPFIIIGQLASISYFS
IILILMPISGIIEDKMLKLYP
Sequence of entity 4 (D, O), FASTA
>7O3E_4 Cytochrome c1, heme protein, mitochondrial (chains D, O)
SDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCSSCHSMDYVAYRHLVGVCYTEEE
AKALAEEVEVQDGPNDDGEMFMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRAR
HGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIGMAPPIYTEVLEYDDGTPATMS
QVAKDVATFLRWASEPEHDHRKRMGLKMLLMMGLLLPLTYAMKRHKWSVLKSRKLAYRPP
K
Sequence of entity 5 (F, Q), FASTA
>7O3E_5 Cytochrome b-c1 complex subunit 7 (chains F, Q)
AGRSAVSASSKWLDGFRKWYYNAAGFNKLGLMRDDTLHETEDVKEAIRRLPEDLYNDRMF
RIKRALDLTMRHQILPKDQWTKYEEDKFYLEPYLKEVIRERKEREEWAKK
Sequence of entity 6 (G, R), FASTA
>7O3E_6 Cytochrome b-c1 complex subunit 8 (chains G, R)
GREFGNLARIRHVISYSLSPFEQRAFPSYFSKGIPNVLRRTRERILRVAPPFVVVYLIYT
WGNQEFEQSKRKNPAMYENDK
Sequence of entity 7 (H, S), FASTA
>7O3E_7 Cytochrome b-c1 complex subunit 6, mitochondrial (chains H, S)
GDPKEEEEEELVDPLTTVREHCEQLEKCVKARERLELCDNRVSSRSQTEEDCTEELFDFL
HARDHCVAHKLFKNLK
Sequence of entity 8 (P), FASTA
>7O3E_8 Cytochrome b-c1 complex subunit Rieske, mitochondrial (chains P)
SHTDVKVPDFSDYRRAEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVS
SMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDP
QHDLDRVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNL
EVPAYEFTSDDVVVVG
Sequence of entity 9 (T), FASTA
>7O3E_9 Cytochrome b-c1 complex subunit 9 (chains T)
MLSVAARSGPFAPVLSATSRGVAGALRPLLQGAVPAASEPPVLDVKRPFLCRESLSGQAA
ARPLVATVGLNVPASVRF
Sequence of entity 10 (I), FASTA
>7O3E_10 Cox7a2l protein (chains I)
MYYKFSSFTQKLAGAWASEAYTPQGLKPVSTEAPPIIFATPTKLTSSVTAYDYSGKNKVP
ELQKFFQKADGVPIHLKRGLPDQMLYRTTMALTLGGTIYCLIALYMASQPRNK
Sequence of entity 11 (a), FASTA
>7O3E_11 Cytochrome c oxidase subunit 1 (chains a)
MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVIVTA
HAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEA
GAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQ
TPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH
PEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVD
TRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLSN
SSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFSGFTLDDTWAKAHFAIMFVG
VNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVLIMIFMIWEAFASKR
EVMSVSYASTNLEWLHGCPPPYHTFEEPTYVKVK
Sequence of entity 12 (b), FASTA
>7O3E_12 Cytochrome c oxidase subunit 2 (chains b)
MAYPFQLGLQDATSPIMEELMNFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQE
VETIWTILPAVILIMIALPSLRILYMMDEINNPVLTVKTMGHQWYWSYEYTDYEDLCFDS
YMIPTNDLKPGELRLLEVDNRVVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLN
QATVTSNRPGLFYGQCSEICGSNHSFMPIVLEMVPLKYFENWSASMI
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| TGL | Tristearoylglycerol | C57 H110 O6 | 1 |
| ZN | Zinc ion | Zn | 1 |
| CUA | Dinuclear copper ion | Cu2 | 1 |
| MG | Magnesium ion | Mg | 1 |
| HEA | Heme-a | C49 H56 Fe N4 O6 | 2 |
| CU | Copper (II) ion | Cu | 1 |
| PC1 | 1,2-diacyl-sn-glycero-3-phosphocholine | C44 H88 N O8 P | 2 |
| HEC | Heme C | C34 H36 Fe N4 O4 | 2 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 5 |
| 3PE | 1,2-Distearoyl-sn-glycerophosphoethanolamine | C41 H82 N O8 P | 13 |
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 4 |
Water and common crystallization additives (NA) are not listed.
Primary citation
Structure and assembly of the mammalian mitochondrial supercomplex CIII 2 CIV. Vercellino, I., Sazanov, L.A. Nature (2021) 598:364-367. DOI 10.1038/s41586-021-03927-z · 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
- 8PW6 3.3 Å, C respirasome from murine liver
- 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
- 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
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