4pd4

Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action

Method: X-RAY DIFFRACTION

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cytochrome b-c1 complex subunit 1, mitochondrial

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （P07257） Cytochrome b × 2 （P00163） Cytochrome c1, heme protein, mitochondrial × 2 （P07143） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （P08067） Cytochrome b-c1 complex subunit 6 × 2 （P00127） Cytochrome b-c1 complex subunit 7 × 2 （P00128） Cytochrome b-c1 complex subunit 8 × 2 （P08525） Cytochrome b-c1 complex subunit 9 × 2 （P22289） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	QCR1_YEAST
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–431； UniProt 27–457

Cytochrome b-c1 complex subunit 2, mitochondrial

OrganismNot specified

UniProt P07257

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 1, mitochondrial × 2 （P07256） Cytochrome b × 2 （P00163） Cytochrome c1, heme protein, mitochondrial × 2 （P07143） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （P08067） Cytochrome b-c1 complex subunit 6 × 2 （P00127） Cytochrome b-c1 complex subunit 7 × 2 （P00128） Cytochrome b-c1 complex subunit 8 × 2 （P08525） Cytochrome b-c1 complex subunit 9 × 2 （P22289） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	QCR2_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–352； UniProt 17–368

Cytochrome b

OrganismNot specified

UniProt P00163

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 1, mitochondrial × 2 （P07256） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （P07257） Cytochrome c1, heme protein, mitochondrial × 2 （P07143） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （P08067） Cytochrome b-c1 complex subunit 6 × 2 （P00127） Cytochrome b-c1 complex subunit 7 × 2 （P00128） Cytochrome b-c1 complex subunit 8 × 2 （P08525） Cytochrome b-c1 complex subunit 9 × 2 （P22289） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CYB_YEAST
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–385； UniProt 1–385

Cytochrome c1, heme protein, mitochondrial

OrganismNot specified

UniProt P07143

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 1, mitochondrial × 2 （P07256） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （P07257） Cytochrome b × 2 （P00163） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （P08067） Cytochrome b-c1 complex subunit 6 × 2 （P00127） Cytochrome b-c1 complex subunit 7 × 2 （P00128） Cytochrome b-c1 complex subunit 8 × 2 （P08525） Cytochrome b-c1 complex subunit 9 × 2 （P22289） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CY1_YEAST
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–248； UniProt 62–309

Cytochrome b-c1 complex subunit Rieske, mitochondrial

OrganismNot specified

UniProt P08067

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 1, mitochondrial × 2 （P07256） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （P07257） Cytochrome b × 2 （P00163） Cytochrome c1, heme protein, mitochondrial × 2 （P07143） Cytochrome b-c1 complex subunit 6 × 2 （P00127） Cytochrome b-c1 complex subunit 7 × 2 （P00128） Cytochrome b-c1 complex subunit 8 × 2 （P08525） Cytochrome b-c1 complex subunit 9 × 2 （P22289） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	UCRI_YEAST
Isoform	—
PDB entities	5
Chains and sequence ranges	Author chain E； PDBConstruct 1–185； UniProt 31–215

Cytochrome b-c1 complex subunit 6

OrganismNot specified

UniProt P00127

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 1, mitochondrial × 2 （P07256） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （P07257） Cytochrome b × 2 （P00163） Cytochrome c1, heme protein, mitochondrial × 2 （P07143） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （P08067） Cytochrome b-c1 complex subunit 7 × 2 （P00128） Cytochrome b-c1 complex subunit 8 × 2 （P08525） Cytochrome b-c1 complex subunit 9 × 2 （P22289） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	QCR6_YEAST
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain F； PDBConstruct 1–74； UniProt 74–147

Cytochrome b-c1 complex subunit 7

OrganismNot specified

UniProt P00128

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 1, mitochondrial × 2 （P07256） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （P07257） Cytochrome b × 2 （P00163） Cytochrome c1, heme protein, mitochondrial × 2 （P07143） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （P08067） Cytochrome b-c1 complex subunit 6 × 2 （P00127） Cytochrome b-c1 complex subunit 8 × 2 （P08525） Cytochrome b-c1 complex subunit 9 × 2 （P22289） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	QCR7_YEAST
Isoform	—
PDB entities	7
Chains and sequence ranges	Author chain G； PDBConstruct 1–126； UniProt 2–127

Cytochrome b-c1 complex subunit 8

OrganismNot specified

UniProt P08525

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 1, mitochondrial × 2 （P07256） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （P07257） Cytochrome b × 2 （P00163） Cytochrome c1, heme protein, mitochondrial × 2 （P07143） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （P08067） Cytochrome b-c1 complex subunit 6 × 2 （P00127） Cytochrome b-c1 complex subunit 7 × 2 （P00128） Cytochrome b-c1 complex subunit 9 × 2 （P22289） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	QCR8_YEAST
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain H； PDBConstruct 1–93； UniProt 2–94

Cytochrome b-c1 complex subunit 9

OrganismNot specified

UniProt P22289

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 22	Cytochrome b-c1 complex subunit 1, mitochondrial × 2 （P07256） Cytochrome b-c1 complex subunit 2, mitochondrial × 2 （P07257） Cytochrome b × 2 （P00163） Cytochrome c1, heme protein, mitochondrial × 2 （P07143） Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 （P08067） Cytochrome b-c1 complex subunit 6 × 2 （P00127） Cytochrome b-c1 complex subunit 7 × 2 （P00128） Cytochrome b-c1 complex subunit 8 × 2 （P08525） Igh protein × 2 Ig kappa chain V-V region HP 124E1 × 2 UNDECYL-MALTOSIDE × 2 1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE × 6 PROTOPORPHYRIN IX CONTAINING FE × 6 2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione × 2 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 FE2/S2 (INORGANIC) CLUSTER × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	QCR9_YEAST
Isoform	—
PDB entities	9
Chains and sequence ranges	Author chain I； PDBConstruct 1–57； UniProt 2–58

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	4pd4
Deposition date deposition_date	2014-04-17
Structure title title	Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action
Keywords keywords	Cytochrome bc1 complex, Membrane protein complex, antimalarial drug, inhibitor, OXIDOREDUCTASE-INHIBITOR complex; OXIDOREDUCTASE/INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

4pd4__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

4pd4__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4pd4__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	58.87 Å
Rg (electron density)	57.97 Å
Total Rg	58.01 Å
Atom count	35292
Residues	4370
Excluded volume	632880 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4pd4__assembly_1__model_1`	22-meric （22）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (18)

Entity 1 Entity 1 polymer

Description description	Cytochrome b-c1 complex subunit 1, mitochondrial
Molecular weight formula_weight	47445.2 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	17646

AEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQVQDFEDNDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEGEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSLSYKDSGLWGFSTATRNVTMIDDLIHFTLKQWNRLTISVTDTEVERAKSLLKLQLGQLYESGNPVNDANLLGAEVLIKGSKLSLGEAFKKIDAITVKDVKAWAGKRLWDQDIAIAGTGQIEGLLDYMRIRSDMSMMRW

Entity 2 Entity 2 polymer

Description description	Cytochrome b-c1 complex subunit 2, mitochondrial
Molecular weight formula_weight	38751.9 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B

LTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQCPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVLANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSPAINYTKLKNAVQNESVSSPIELNFDAVKDFKLGKFNYVAVGDVSNLPYLDEL

Entity 3 Entity 3 polymer

Description description	Cytochrome b
Molecular weight formula_weight	43686.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C

MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGHPDNYIPGNPLVTPASIVPEWYLLPFYAILRSIPDKLLGVITMFAAILVLLVLPFTDRSVVRGNTFKVLSKFFFFIFVFNFVLLGQIGACHVEVPYVLMGQIATFIYFAYFLIIVPVISTIENVLFYIGRVNK

Entity 4 Entity 4 polymer

Description description	Cytochrome c1, heme protein, mitochondrial
Molecular weight formula_weight	27807.4 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D

MTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFVFNPPKPRK

Entity 5 Entity 5 polymer

Description description	Cytochrome b-c1 complex subunit Rieske, mitochondrial
Molecular weight formula_weight	20123.0 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E

KSTYRTPNFDDVLKENNDADKGRSYAYFMVGAMGLLSSAGAKSTVETFISSMTATADVLAMAKVEVNLAAIPLGKNVVVKWQGKPVFIRHRTPHEIQEANSVDMSALKDPQTDADRVKDPQWLIMLGICTHLGCVPIGEAGDFGGWFCPCHGSHYDISGRIRKGPAPLNLEIPAYEFDGDKVIVG

Entity 6 Entity 6 polymer

Description description	Cytochrome b-c1 complex subunit 6
Molecular weight formula_weight	8854.8 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F

VTDQLEDLREHFKNTEEGKALVHHYEECAERVKIQQQQPGYADLEHKEDCVEEFFHLQHYLDTATAPRLFDKLK

Entity 7 Entity 7 polymer

Description description	Cytochrome b-c1 complex subunit 7
Molecular weight formula_weight	14452.6 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G

PQSFTSIARIGDYILKSPVLSKLCVPVANQFINLAGYKKLGLKFDDLIAEENPIMQTALRRLPEDESYARAYRIIRAHQTELTHHLLPRNEWIKAQEDVPYLLPYILEAEAAAKEKDELDNIEVSK

Entity 8 Entity 8 polymer

Description description	Cytochrome b-c1 complex subunit 8
Molecular weight formula_weight	10856.3 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H

GPPSGKTYMGWWGHMGGPKQKGITSYAVSPYAQKPLQGIFHNAVFNSFRRFKSQFLYVLIPAGIYWYWWKNGNEYNEFLYSKAGREELERVNV

Entity 9 Entity 9 polymer

Description description	Cytochrome b-c1 complex subunit 9
Molecular weight formula_weight	6535.5 kDa
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I

SFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKARIAA

Entity 10 Entity 10 polymer

Description description	Igh protein
Molecular weight formula_weight	14365.8 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J

EVKLQESGAGLVQPSQSLSLTCSVTGYSITSGYYWNWIRLFPGNKLEWVGYISNVGDNNYNPSLKDRLSITRDTSKNQFFLKLNSVTTEDTATYYCARSEYYSVTGYAMDYWGQGTTVTVSSAWRHP

Source Source

Source organism organism	Mus musculus
Common name common_name	Mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090
Host organism host_organism	Escherichia coli

Entity 11 Entity 11 polymer

Description description	Ig kappa chain V-V region HP 124E1
Molecular weight formula_weight	11926.4 kDa
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K

DIELTQTPVSLAASLGDRVTISCRASQDINNFLNWYQQKPDGTIKLLIYYTSRLHAGVPSRFSGSGSGTDYSLTISNLEPEDIATYFCQHHIKFPWTFGAGTKLEIK

Source Source

Source organism organism	Mus musculus
Common name common_name	Mouse
NCBI taxonomy ID ncbi_taxonomy_id	10090
Host organism host_organism	Escherichia coli

Entity 12 Entity 12 non-polymer

Description description	UNDECYL-MALTOSIDE
Molecular weight formula_weight	496.6 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 13 Entity 13 non-polymer

Description description	1,2-DIACYL-GLYCEROL-3-SN-PHOSPHATE
Molecular weight formula_weight	705.0 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 14 Entity 14 non-polymer

Description description	PROTOPORPHYRIN IX CONTAINING FE
Molecular weight formula_weight	616.5 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 15 Entity 15 non-polymer

Description description	2-[trans-4-(4-chlorophenyl)cyclohexyl]-3-hydroxynaphthalene-1,4-dione
Molecular weight formula_weight	366.8 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 16 Entity 16 non-polymer

Description description	1,2-Distearoyl-sn-glycerophosphoethanolamine
Molecular weight formula_weight	748.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 17 Entity 17 non-polymer

Description description	5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL
Molecular weight formula_weight	592.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 18 Entity 18 non-polymer

Description description	FE2/S2 (INORGANIC) CLUSTER
Molecular weight formula_weight	175.8 kDa
Source method src_method	syn
Copy count entity_count	1

▼

6. Fold Classification (SCOP + CATH) 31 domains

SCOP 2.08 (16 domains)

Domain ID domain_id	d4pd4a1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d4pd4a2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d4pd4b1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d4pd4b2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamily	d.185.1 — LuxS/MPP-like metallohydrolase
Family Family family	d.185.1.1 — MPP-like

Domain ID domain_id	d4pd4c1
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.21 — Heme-binding four-helical bundle
Superfamily Superfamily superfamily	f.21.1 — Transmembrane di-heme cytochromes
Family Family family	f.21.1.2 — Cytochrome b of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d4pd4c2
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.32 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamily	f.32.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.32.1.0 — automated matches

Domain ID domain_id	d4pd4d1
Class class	a — All alpha proteins
Fold Fold fold	a.3 — Cytochrome c
Superfamily Superfamily superfamily	a.3.1 — Cytochrome c
Family Family family	a.3.1.3 — Cytochrome bc1 domain

Domain ID domain_id	d4pd4d2
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.11 — Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor
Family Family family	f.23.11.0 — automated matches

Domain ID domain_id	d4pd4e1
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.12 — ISP transmembrane anchor
Family Family family	f.23.12.0 — automated matches

Domain ID domain_id	d4pd4e2
Class class	b — All beta proteins
Fold Fold fold	b.33 — ISP domain
Superfamily Superfamily superfamily	b.33.1 — ISP domain
Family Family family	b.33.1.1 — Rieske iron-sulfur protein (ISP)

Domain ID domain_id	d4pd4f_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.28 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamily	f.28.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.28.1.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d4pd4g_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.27 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamily	f.27.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.27.1.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d4pd4h_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.13 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.23.13.1 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d4pd4i_
Class class	f — Membrane and cell surface proteins and peptides
Fold Fold fold	f.23 — Single transmembrane helix
Superfamily Superfamily superfamily	f.23.14 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family family	f.23.14.1 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d4pd4j_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

Domain ID domain_id	d4pd4k_
Class class	b — All beta proteins
Fold Fold fold	b.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamily	b.1.1 — Immunoglobulin
Family Family family	b.1.1.1 — V set domains (antibody variable domain-like)

CATH v4.4 (15 domains)

Domain ID domain_id	4pd4A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	4pd4A02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	4pd4B01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	4pd4B02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Metalloenzyme, LuxS/M16 peptidase-like

Domain ID domain_id	4pd4C00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	810 — Cytochrome Bc1 Complex; Chain C
Homologous superfamily homologous superfamily	10 — Cytochrome Bc1 Complex; Chain C

Domain ID domain_id	4pd4D01
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily	10 — Cytochrome c-like domain

Domain ID domain_id	4pd4D02
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	100 — Cytochrome c1, transmembrane anchor, C-terminal

Domain ID domain_id	4pd4E01
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	270 — Ubiquinol cytochrome reductase, transmembrane domain

Domain ID domain_id	4pd4E02
Class class	2 — Mainly Beta
Architecture architecture	102 — 3-layer Sandwich
Topology topology	10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily	10 — Rieske [2Fe-2S] iron-sulphur domain

Domain ID domain_id	4pd4F00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	20 — Ubiquinol-cytochrome C reductase hinge domain

Domain ID domain_id	4pd4G00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	1090 — Cytochrome Bc1 Complex; Chain F
Homologous superfamily homologous superfamily	10 — Cytochrome b-c1 complex subunit 7

Domain ID domain_id	4pd4H00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	210 — Cytochrome b-c1 complex subunit 8

Domain ID domain_id	4pd4I00
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily	260 — Cytochrome b-c1 complex subunit 9

Domain ID domain_id	4pd4J00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

Domain ID domain_id	4pd4K00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	10 — Immunoglobulins

▶

Unit-cell length a length_a	212.260 Å
Unit-cell length b length_b	150.880 Å
Unit-cell length c length_c	143.090 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	115.18 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	3.040 Å
Low-resolution limit resolution_low	24.989 Å
R factor r_factor	0.2691
R_work r_work	0.2683
R_free r_free	0.2966

Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action

1. Protein Identity and Related Structures Protein Identity & Related Structures

Cytochrome b-c1 complex subunit 1, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cytochrome b-c1 complex subunit 2, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cytochrome b

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cytochrome c1, heme protein, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cytochrome b-c1 complex subunit Rieske, mitochondrial

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cytochrome b-c1 complex subunit 6

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cytochrome b-c1 complex subunit 7

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cytochrome b-c1 complex subunit 8

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Cytochrome b-c1 complex subunit 9

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

4pd4__assembly_1__model_1

4pd4__assembly_1__model_1 | I(q)

4pd4__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment