4PD4: Cytochrome b-c1 complex subunit 1, mitochondrial

Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action. Determined by X-ray diffraction at 3.04 Å resolution. Released 11 Jun 2014.

Method
X-ray diffraction
Resolution
3.04 Å
Organisms
Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Mus musculus
Chains
11
Atoms
17,646
Mol. weight
251.15 kDa
Ligands
UMQ, 3PH, HEM, AOQ
Released
11 Jun 2014

Explore 4PD4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PD4 contains 103 α-helices and 85 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: 23 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand30-3341
β-strand37-4261
β-strand49-5571
α-helix69-768
α-helix80-889
β-strand92-9761
β-strand102-10871
α-helix114-1218
α-helix122-1265
α-helix137-1404
α-helix144-1474
α-helix151-1544
α-helix156-16813
α-helix173-1753
α-helix190-20011
β-strand206-21271
α-helix216-2238
α-helix234-2363
α-helix240-2423
β-strand247-25262
β-strand259-26682
α-helix275-28511
β-strand287-28932
α-helix293-2964
α-helix302-3065
β-strand314-32182
β-strand326-33492
α-helix340-35617
α-helix360-37819
α-helix383-39614
α-helix403-41210
α-helix415-42511
β-strand431-43772
α-helix445-4484
α-helix449-4524
Chain B: 22 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand18-1923
β-strand2214
β-strand28-3035
β-strand33-3533
β-strand3616
α-helix39-413
α-helix47-526
β-strand5917
α-helix64-7411
β-strand77-7825
β-strand81-8228
β-strand8616
β-strand87-8828
β-strand91-9445
α-helix95-973
α-helix98-11114
β-strand11217
α-helix116-1183
α-helix119-1235
α-helix124-13411
α-helix138-14912
α-helix170-17910
α-helix182-1843
β-strand185-18733
β-strand19014
α-helix194-20310
α-helix205-2084
α-helix220-2223
β-strand228-23259
β-strand237-24269
α-helix250-26011
α-helix266-2694
β-strand273-27869
β-strand283-29199
α-helix294-2996
α-helix304-3107
β-strand312-313210
α-helix315-3173
α-helix320-3267
β-strand345-346210
β-strand352-35769
α-helix359-3613
α-helix365-3673
Chain C: 20 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix3-64
α-helix10-145
β-strand21-23311
α-helix31-5121
α-helix58-7013
α-helix75-10228
α-helix111-13323
α-helix138-14912
α-helix158-1647
α-helix173-20230
β-strand218-220311
α-helix224-24623
α-helix254-2574
α-helix276-2838
α-helix288-30013
α-helix301-3033
α-helix305-3084
α-helix316-3183
α-helix320-34122
α-helix348-36114
α-helix362-3665
α-helix367-38014
Chain D: 11 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix64-674
α-helix87-9913
α-helix101-1033
β-strand111112
α-helix112-1154
β-strand116113
β-strand120113
α-helix122-1309
β-strand154112
α-helix162-1676
α-helix174-1763
α-helix188-1958
β-strand213-214214
β-strand222-223214
α-helix226-2272
α-helix247-25913
α-helix263-29634
β-strand29912
β-strand302115
Chain E: 7 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix36-383
α-helix44-452
α-helix51-8030
α-helix84-852
β-strand95-97316
β-strand106-111617
β-strand114-120717
α-helix123-1297
α-helix143-1464
β-strand152-156517
α-helix1661
β-strand167-170418
β-strand174-178518
β-strand183-186418
β-strand191118
β-strand206-208316
β-strand211-213316
Chain F: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix79-868
α-helix89-11022
α-helix114-1163
α-helix124-13815
α-helix142-1454
Chain G: 7 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix5-1713
α-helix19-3517
α-helix38-414
α-helix45-484
α-helix54-585
α-helix65-8420
α-helix104-12219
Chain H: 4 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix4-74
β-strand24115
β-strand26-2942
α-helix50-7930
α-helix83-853
α-helix86-927

3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cytochrome b-c1 complex subunit 1, mitochondrialAprotein431Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P07256 (AlphaFold model)
Cytochrome b-c1 complex subunit 2, mitochondrialBprotein352Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P07257 (AlphaFold model)
Cytochrome bCprotein385Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P00163 (AlphaFold model)
Cytochrome c1, heme protein, mitochondrialDprotein248Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P07143 (AlphaFold model)
Cytochrome b-c1 complex subunit Rieske, mitochondrialEprotein185Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P08067
Cytochrome b-c1 complex subunit 6Fprotein74Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P00127
Cytochrome b-c1 complex subunit 7Gprotein126Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P00128
Cytochrome b-c1 complex subunit 8Hprotein93Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P08525
Cytochrome b-c1 complex subunit 9Iprotein57Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P22289
Igh proteinJprotein127Mus musculusQ53VQ5
Ig kappa chain V-V region HP 124E1Kprotein107Mus musculusP01647
Sequence of entity 1 (A), FASTA
>4PD4_1 Cytochrome b-c1 complex subunit 1, mitochondrial (chains A)
AEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVA
AKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLK
QVQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNA
VVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVE
GEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSG
LWGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVND
ANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYM
RIRSDMSMMRW
Sequence of entity 2 (B), FASTA
>4PD4_2 Cytochrome b-c1 complex subunit 2, mitochondrial (chains B)
LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGG
TFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQ
CPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEAD
LKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVL
ANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSP
AINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL
Sequence of entity 3 (C), FASTA
>4PD4_3 Cytochrome b (chains C)
MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIEL
AFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVII
FILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFF
ALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLIL
ALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAIL
VLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYF
AYFLIIVPVISTIENVLFYIGRVNK
Sequence of entity 4 (D), FASTA
>4PD4_4 Cytochrome c1, heme protein, mitochondrial (chains D)
MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHT
NEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIV
KARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTP
ATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFV
FNPPKPRK
Sequence of entity 5 (E), FASTA
>4PD4_5 Cytochrome b-c1 complex subunit Rieske, mitochondrial (chains E)
KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLA
MAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDP
QWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGD
KVIVG
Sequence of entity 6 (F), FASTA
>4PD4_6 Cytochrome b-c1 complex subunit 6 (chains F)
VTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQHY
LDTATAPRLFDKLK
Sequence of entity 7 (G), FASTA
>4PD4_7 Cytochrome b-c1 complex subunit 7 (chains G)
PQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALR
RLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELD
NIEVSK
Sequence of entity 8 (H), FASTA
>4PD4_8 Cytochrome b-c1 complex subunit 8 (chains H)
GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVLI
PAGIYWYWWKNGNEYNEFLYSKAGREELERVNV
Sequence of entity 9 (I), FASTA
>4PD4_9 Cytochrome b-c1 complex subunit 9 (chains I)
SFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKARIAA
Sequence of entity 10 (J), FASTA
>4PD4_10 Igh protein (chains J)
EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRLFPGNKLEWVGYISNVGDNNY
NPSLKDRLSITRDTSKNQFFLKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTV
SSAWRHP
Sequence of entity 11 (K), FASTA
>4PD4_11 Ig kappa chain V-V region HP 124E1 (chains K)
DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKPDGTIKLLIYYTSRLHAGVPS
RFSGSGSGTDYSLTISNLEPEDIATYFCQHHIKFPWTFGAGTKLEIK

Ligands and cofactors

IDNameFormulaCopies
UMQUndecyl-maltosideC23 H44 O111
3PH1,2-diacyl-glycerol-3-sn-phosphateC39 H77 O8 P3
HEMProtoporphyrin IX containing FEC34 H32 Fe N4 O43
AOQ2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dioneC22 H19 Cl O31
3PE1,2-Distearoyl-sn-glycerophosphoethanolamineC41 H82 N O8 P1
UQ65-(3,7,11,15,19,23-hexamethyl-tetracosa-2,6,10,14,18,22-hexaenyl)-2,3-dimethoxy…C39 H60 O41
FESFE2/S2 (inorganic) clusterFe2 S21

Primary citation

Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action. Birth, D., Kao, W.C., Hunte, C. Nat Commun (2014) 5:4029-4029. DOI 10.1038/ncomms5029 · PubMed

Other PDB entries of the same protein (UniProt P07256 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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