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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