1EZV: PDB entry 1EZV

Structure of the yeast cytochrome BC1 complex co-crystallized with an antibody fv-fragment. Determined by X-ray diffraction at 2.3 Å resolution. Released 16 May 2001.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Saccharomyces cerevisiae, Mus musculus
Chains: 11
Atoms: 17,781
Mol. weight: 247.13 kDa
Ligands: HEM, SMA, UQ6, HEC
Released: 16 May 2001

Explore 1EZV in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1EZV contains 112 α-helices and 88 β-strands across 11 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: 21 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	30-33	4	1
β-strand	37-42	6	1
β-strand	48-54	7	1
α-helix	58-60	3
α-helix	68-76	9
α-helix	79-87	9
β-strand	91-96	6	1
β-strand	101-107	7	1
α-helix	109-111	3
α-helix	114-120	7
α-helix	121-125	5
α-helix	133-153	21
α-helix	155-167	13
α-helix	172-174	3
α-helix	181-184	4
α-helix	189-199	11
β-strand	205-211	7	1
α-helix	215-224	10
β-strand	246-251	6	2
β-strand	252	1	3
β-strand	258-265	8	2
α-helix	274-284	11
β-strand	286-288	3	2
α-helix	294-296	3
α-helix	301-306	6
β-strand	313-320	8	2
β-strand	325-333	9	2
α-helix	339-355	17
α-helix	359-377	19
α-helix	382-396	15
α-helix	402-410	9
α-helix	414-424	11
β-strand	431-436	6	2
α-helix	444-449	6

Chain B: 17 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	20	1	4
β-strand	22	1	5
β-strand	28-35	8	6
α-helix	47-54	8
β-strand	59	1	7
α-helix	64-74	11
β-strand	76-82	7	6
β-strand	87-94	8	6
α-helix	95-97	3
α-helix	98-111	14
β-strand	112	1	7
α-helix	116-118	3
α-helix	119-123	5
α-helix	124-134	11
α-helix	138-150	13
β-strand	151	1	8
α-helix	169-179	11
α-helix	182-184	3
β-strand	185-187	3	6
β-strand	188	1	4
β-strand	190	1	6
β-strand	192	1	5
α-helix	194-202	9
α-helix	220-221	2
β-strand	223	1	8
β-strand	228-232	5	9
β-strand	237-245	9	9
α-helix	250-260	11
α-helix	266-270	5
β-strand	273-278	6	9
β-strand	283-291	9	9
α-helix	294-309	16
α-helix	320-324	5
β-strand	352-357	6	9
α-helix	359-361	3

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	10
α-helix	28-31	4
α-helix	32-51	20
α-helix	61-70	10
α-helix	75-103	29
α-helix	111-134	24
β-strand	137	1	11
α-helix	138-149	12
α-helix	150-153	4
α-helix	158-166	9
α-helix	173-204	32
β-strand	218-220	3	10
α-helix	221-225	5
α-helix	226-241	16
α-helix	242-246	5
α-helix	254-257	4
β-strand	259	1	11
α-helix	273-275	3
α-helix	276-283	8
α-helix	288-300	13
α-helix	301-304	4
α-helix	305-308	4
α-helix	320-340	21
α-helix	346-361	16
α-helix	362-366	5
α-helix	367-380	14

Chain D: 15 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	64-67	4
α-helix	69-72	4
α-helix	83-85	3
α-helix	87-99	13
α-helix	101-103	3
β-strand	111	1	12
α-helix	112-114	3
β-strand	116	1	13
β-strand	120	1	13
α-helix	122-130	9
β-strand	133-135	3	14
β-strand	146-148	3	14
β-strand	154	1	12
α-helix	155-157	3
α-helix	162-167	6
α-helix	187-195	9
α-helix	202-203	2
α-helix	208-209	2
β-strand	213-214	2	15
β-strand	222-223	2	15
α-helix	226-227	2
α-helix	244-259	16
α-helix	263-296	34
β-strand	299-302	4	2

Chain E: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	36-38	3
β-strand	43	1	16
α-helix	51-80	30
α-helix	86-88	3
β-strand	94-97	4	17
α-helix	98-100	3
β-strand	106-111	6	18
β-strand	114-120	7	18
α-helix	123-130	8
α-helix	134-136	3
α-helix	143-146	4
β-strand	152-156	5	18
α-helix	164-166	3
β-strand	167-168	2	19
β-strand	176-178	3	19
β-strand	183-185	3	19
β-strand	191-193	3	19
α-helix	199-204	6
β-strand	205-208	4	17
β-strand	211-214	4	17

Chain F: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	5-17	13
α-helix	19-36	18
α-helix	38-41	4
α-helix	45-48	4
α-helix	54-62	9
α-helix	65-83	19
α-helix	90-92	3
α-helix	94-95	2
α-helix	104-121	18

Chain G: 5 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	12	1	20
β-strand	15	1	20
α-helix	19-21	3
β-strand	22	1	3
β-strand	24-29	6	2
α-helix	31-33	3
β-strand	34	1	16
α-helix	56-81	26
α-helix	83-85	3
α-helix	86-92	7

Chain H: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	77-86	10
α-helix	89-109	21
α-helix	124-138	15
α-helix	142-144	3

3 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
Ubiquinol-cytochrome C reductase complex core protein I	A	protein	430	Saccharomyces cerevisiae	P07256 (AlphaFold model)
Ubiquinol-cytochrome C reductase complex core protein 2	B	protein	352	Saccharomyces cerevisiae	P07257 (AlphaFold model)
Cytochrome B	C	protein	385	Saccharomyces cerevisiae	P00163 (AlphaFold model)
Cytochrome C1	D	protein	245	Saccharomyces cerevisiae	P07143 (AlphaFold model)
Ubiquinol-cytochrome C reductase iron-sulfur subunit	E	protein	185	Saccharomyces cerevisiae	P08067
Ubiquinol-cytochrome C reductase complex 17 kd protein	H	protein	74	Saccharomyces cerevisiae	P00127
Ubiquinol-cytochrome C reductase complex 14 kd protein	F	protein	125	Saccharomyces cerevisiae	P00128
Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein qp-C	G	protein	93	Saccharomyces cerevisiae	P08525
Ubiquinol-cytochrome C reductase complex 7.3 kd protein	I	protein	55	Saccharomyces cerevisiae	P22289
Heavy chain (VH) of fv-fragment	X	protein	127	Mus musculus	P18531
Light chain (VL) of fv-fragment	Y	protein	107	Mus musculus	P01647

Sequence of entity 1 (A), FASTA

>1EZV_1 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I (chains A)
AEVTQLSNGIVVATEHNPAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVAA
KEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQ
VQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNAV
VVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEG
EPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSGL
WGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDA
NLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYMR
IRSDMSMMRW

Sequence of entity 2 (B), FASTA

>1EZV_2 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2 (chains B)
LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGG
TFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ
CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEAD
LKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL
ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSP
AINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL

Sequence of entity 3 (C), FASTA

>1EZV_3 CYTOCHROME B (chains C)
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIEL
AFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII
FTLTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFF
ALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL
ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAIL
VLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF
AYFLIIVPVISTIENVLFYIGRVNK

Sequence of entity 4 (D), FASTA

>1EZV_4 CYTOCHROME C1 (chains D)
MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHT
NEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV
KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTP
ATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV
FNPPK

Sequence of entity 5 (E), FASTA

>1EZV_5 UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT (chains E)
KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLA
MAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP
QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGD
KVIVG

Sequence of entity 6 (H), FASTA

>1EZV_6 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 17 KD PROTEIN (chains H)
VTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQHY
LDTATAPRLFDKLK

Sequence of entity 7 (F), FASTA

>1EZV_7 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KD PROTEIN (chains F)
QSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALRR
LPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDN
IEVSK

Sequence of entity 8 (G), FASTA

>1EZV_8 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING PROTEIN QP-C (chains G)
GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVLI
PAGIYWYWWKNGNEYNEFLYSKAGREELERVNV

Sequence of entity 9 (I), FASTA

>1EZV_9 UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.3 KD PROTEIN (chains I)
SSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKARIAA

Sequence of entity 10 (X), FASTA

>1EZV_10 HEAVY CHAIN (VH) OF FV-FRAGMENT (chains X)
EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRLFPGNKLEWVGYISNVGDNNY
NPSLKDRLSITRDTSKNQFFLKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV
SSAWRHP

Sequence of entity 11 (Y), FASTA

>1EZV_11 LIGHT CHAIN (VL) OF FV-FRAGMENT (chains Y)
DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKPDGTIKLLIYYTSRLHAGVPS
RFSGSGSGTDYSLTISNLEPEDIATYFCQHHIKFPWTFGAGTKLEIK

Ligands and cofactors

ID	Name	Formula	Copies
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	2
SMA	Stigmatellin a	C30 H42 O7	1
UQ6	5-(3,7,11,15,19,23-hexamethyl-tetracosa-2,6,10,14,18,22-hexaenyl)-2,3-dimethoxy…	C39 H60 O4	1
HEC	Heme C	C34 H36 Fe N4 O4	1
FES	FE2/S2 (inorganic) cluster	Fe2 S2	1

Primary citation

Structure at 2.3 A resolution of the cytochrome bc(1) complex from the yeast Saccharomyces cerevisiae co-crystallized with an antibody Fv fragment. Hunte, C., Koepke, J., Lange, C. et al. Structure (2000) 8:669-684. DOI 10.1016/S0969-2126(00)00152-0 · 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…
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
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

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