3cwb

Chicken Cytochrome BC1 Complex inhibited by an iodinated analogue of the polyketide Crocacin-D

Method: X-RAY DIFFRACTION

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

Cytochrome b

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 20	MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR PROTEIN × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, leader sequence × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 octyl beta-D-glucopyranoside × 6 AZIDE ION × 2 PROTOPORPHYRIN IX CONTAINING FE × 4 methyl N-[(5Z)-6-({[4-(4-iodobenzyl)phenyl]carbonyl}amino)hex-5-enoyl]glycinate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 HEME C × 2 CARDIOLIPIN × 4 FE2/S2 (INORGANIC) CLUSTER × 2 UNKNOWN LIGAND × 4 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	CYB_CHICK
Isoform	—
PDB entities	3
Chains and sequence ranges	Author chain C； PDBConstruct 1–380； UniProt 1–380 Author chain P； PDBConstruct 1–380； UniProt 1–380

MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, leader sequence

OrganismNot specified

UniProt Q5ZLR5

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 20	MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 Cytochrome b × 2 （P18946） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR PROTEIN × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 octyl beta-D-glucopyranoside × 6 AZIDE ION × 2 PROTOPORPHYRIN IX CONTAINING FE × 4 methyl N-[(5Z)-6-({[4-(4-iodobenzyl)phenyl]carbonyl}amino)hex-5-enoyl]glycinate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 HEME C × 2 CARDIOLIPIN × 4 FE2/S2 (INORGANIC) CLUSTER × 2 UNKNOWN LIGAND × 4 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q5ZLR5_CHICK
Isoform	—
PDB entities	9
Chains and sequence ranges	Author chain I； PDBConstruct 21–52； UniProt 45–76 Author chain V； PDBConstruct 21–52； UniProt 45–76

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3cwb
Deposition date deposition_date	2008-04-21
Structure title title	Chicken Cytochrome BC1 Complex inhibited by an iodinated analogue of the polyketide Crocacin-D
Keywords keywords	;Crocacin D, inhibitor design, structure-activity relationship, polyketide, fungicide, CYTOCHROME BC1, MEMBRANE PROTEIN, HEME PROTEIN, RIESKE IRON SULFUR PROTEIN, CYTOCHROME B, CYTOCHROME C1, COMPLEX III, MITOCHONDRIAL PROCESSING PROTEA UBIQUINONE, OXIDOREDUCTASE, REDOX ENZYME, RESPIRATORY CHAIN, Electron transport, Heme, Inner membrane, Iron, Membrane, Metal-binding, Mitochondrion, Transmembrane, Transport ;; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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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.

3cwb__assembly_1__model_1

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

Download this curve (.dat)

3cwb__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3cwb__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	55.26 Å
Rg (electron density)	54.38 Å
Total Rg	54.53 Å
Atom count	32673
Residues	4071
Excluded volume	585030 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3cwb__assembly_1__model_1`	eicosameric （20）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (21)

Entity 1 Entity 1 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I
Molecular weight formula_weight	49503.8 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,N
Atom count atom_count	32696

AATYAQTLQNIPETNVTTLDNGLRVASEESSQPTCTVGVWIGAGSRYENEKNNGAGYFVEHLAFKGTKKRPCAAFEKEVESMGAHFNGYTSREQTAFYIKALSKDMPKVVELLADVVQNCALEESQIEKERGVILQELKEMDNDMTNVTFDYLHATAFQGTALARTVEGTTENIKHLTRADLASYIDTHFKAPRMVLAAAGGISHKELVDAARQHFSGVSFTYKEDAVPILPRCRFTGSEIRARDDALPVAHVALAVEGPGWADPDNVVLHVANAIIGRYDRTFGGGKHLSSRLAALAVEHKLCHSFQTFNTSYSDTGLFGFHFVADPLSIDDMMFCAQGEWMRLCTSTTESEVKRAKNHLRSAMVAQLDGTTPVCETIGSHLLNYGRRISLEEWDSRISAVDARMVRDVCSKYIYDKCPALAAVGPIEQLLDYNRIRSGMYWIRF

Entity 2 Entity 2 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2
Molecular weight formula_weight	46683.8 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,O

SLKVAPKVAVSAAAERVKLCPGAEDLEITKLPNGLIIASLENFSPASRIGVFIKAGSRYETTANLGTAHLLRLASPLTTKGASSFRITRGIEAVGGSLSVYSTREKMTYCVECLRDHVDTVMEYLLNVTTAPEFRPWEVTDLQPQLKVDKAVAFQSPQVGVLENLHAAAYKTALANPLYCPDYRIGKITSEQLHHFVQNNFTSARMALVGIGVKHSDLKQVAEQFLNIRSGAGTSSAKATYWGGEIREQNGHSLVHAAVVTEGAAVGSAEANAFSVLQHVLGAGPLIKRGSSVTSKLYQGVAKATTQPFDASAFNVNYSDSGLFGFYTISQAAHAGEVIRAAMNQLKAAAQGGVTEEDVTKAKNQLKATYLMSVETAQGLLNEIGSEALLSGTHTAPSVVAQKIDSVTSADVVNAAKKFVSGKKSMAASGDLGSTPFLDEL

Entity 3 Entity 3 polymer

Description description	Cytochrome b
Molecular weight formula_weight	42623.0 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,P

MAPNIRKSHPLLKMINNSLIDLPAPSNISAWWNFGSLLAVCLMTQILTGLLLAMHYTADTSLAFSSVAHTCRNVQYGWLIRNLHANGASFFFICIFLHIGRGLYYGSYLYKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGHTLVEWAWGGFSVDNPTLTRFFALHFLLPFAIAGITIIHLTFLHESGSNNPLGISSDSDKIPFHPYYSFKDILGLTLMLTPFLTLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLILFLIPFLHKSKQRTMTFRPLSQTLFWLLVANLLILTWIGSQPVEHPFIIIGQMASLSYFTILLILFPTIGTLENKMLNY

Entity 4 Entity 4 polymer

Description description	MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN
Molecular weight formula_weight	26973.7 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,Q

GELELHPPAFPWSHGGPLSALDHSSVRRGFQVYKQVCSACHSMDYVAFRNLIGVTHTEAEAKALAEEVEVQDGPDENGELFMRPGKISDYFPKPYPNPEAARAANNGALPPDLSYIVNARHGGEDYVFSLLTGYCDPPAGVVVREGLHYNPYFPGQAIGMAPPIYNEILEYDDGTPATMSQIAKDVCTFLRWAAEPEHDQRKRMGLKMLLISALLTSLLYYMKRHKWSVLKSRKMAYRPPK

Entity 5 Entity 5 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR PROTEIN
Molecular weight formula_weight	21506.2 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,R

VHNDVTVPDFSAYRREDVMDATTSSQTSSEDRKGFSYLVTATACVATAYAAKNVVTQFISSLSASADVLALSKIEIKLSDIPEGKNVAFKWRGKPLFVRHRTQAEINQEAEVDVSKLRDPQHDLDRVKKPEWVILVGVCTHLGCVPIANSGDFGGYYCPCHGSHYDASGRIRKGPAPYNLEVPTYQFVGDDLVVVG

Entity 6 Entity 6 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN
Molecular weight formula_weight	13394.5 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,S

AARATVAGGGRLMDRIRKWYYNAAGFNKYGLMRDDTLYEDDDVKEALKRLPKDLYNERMFRIKRALDLSLKHRILPKEQWVKYEEDKPYLEPYLKEVIRERLEREAWNKK

Entity 7 Entity 7 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C
Molecular weight formula_weight	9498.7 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,T

GIHFGNLARVRHIITYSLSPFEQRAIPNIFSDALPNVWRRFSSQVFKVAPPFLGAYLLYSWGTQEFERLKRKNPADYENDQ

Entity 8 Entity 8 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII
Molecular weight formula_weight	9057.1 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,U

LRGSGEEEEEELVDPLTTIREHCEQTEKCVKARERLELCDARVSSRSHTEEQCTEELFDFLHARDHCVAHKLFNKLK

Entity 9 Entity 9 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, leader sequence
Molecular weight formula_weight	5211.2 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,V

XXXXXXXXXXXXXXXXXXXXRPLLCRESMSGRSARRDLVAGISLNAPASVRY

Entity 10 Entity 10 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN
Molecular weight formula_weight	7006.0 kDa
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J,W

ALLRQAYSALFRRTSTFALTVVLGAVLFERAFDQGADAIFEHLNEGKLWKHIKHKYEASEE

Entity 11 Entity 11 non-polymer

Description description	1,2-dioleoyl-sn-glycero-3-phosphoethanolamine
Molecular weight formula_weight	744.0 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 12 Entity 12 non-polymer

Description description	octyl beta-D-glucopyranoside
Molecular weight formula_weight	292.4 kDa
Source method src_method	man
Copy count entity_count	6

Entity 13 Entity 13 non-polymer

Description description	AZIDE ION
Molecular weight formula_weight	42.0 kDa
Source method src_method	syn
Copy count entity_count	2

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	4

Entity 15 Entity 15 non-polymer

Description description	methyl N-[(5Z)-6-({[4-(4-iodobenzyl)phenyl]carbonyl}amino)hex-5-enoyl]glycinate
Molecular weight formula_weight	520.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 16 Entity 16 non-polymer

Description description	Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer
Molecular weight formula_weight	863.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 17 Entity 17 non-polymer

Description description	HEME C
Molecular weight formula_weight	618.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 18 Entity 18 non-polymer

Description description	CARDIOLIPIN
Molecular weight formula_weight	1464.0 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 19 Entity 19 non-polymer

Description description	FE2/S2 (INORGANIC) CLUSTER
Molecular weight formula_weight	175.8 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 20 Entity 20 non-polymer

Description description	UNKNOWN LIGAND
Source method src_method	syn
Copy count entity_count	4

Entity 21 Entity 21 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	16

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6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3cwbc1
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.32.1.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d3cwbc2
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	d3cwbp1
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.32.1.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

Domain ID domain_id	d3cwbp2
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)

CATH v4.4 (28 domains)

Domain ID domain_id	3cwbA01
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	3cwbA02
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	3cwbB01
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	3cwbB02
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	3cwbC00
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	3cwbD01
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	3cwbD02
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	3cwbE01
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	3cwbE02
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	3cwbF00
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	3cwbG00
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	3cwbH00
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	3cwbI00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	210 — Cytochrome Bc1 Complex; Chain I
Homologous superfamily homologous superfamily	10 — Cytochrome Bc1 Complex; Chain I

Domain ID domain_id	3cwbJ00
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	3cwbN01
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	3cwbN02
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	3cwbO01
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	3cwbO02
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	3cwbP00
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	3cwbQ01
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	3cwbQ02
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	3cwbR01
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	3cwbR02
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	3cwbS00
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	3cwbT00
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	3cwbU00
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	3cwbV00
Class class	2 — Mainly Beta
Architecture architecture	10 — Ribbon
Topology topology	210 — Cytochrome Bc1 Complex; Chain I
Homologous superfamily homologous superfamily	10 — Cytochrome Bc1 Complex; Chain I

Domain ID domain_id	3cwbW00
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

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Unit-cell length a length_a	174.778 Å
Unit-cell length b length_b	182.663 Å
Unit-cell length c length_c	242.945 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	3.510 Å
Low-resolution limit resolution_low	21.980 Å
R factor r_factor	0.2850
R_work r_work	0.2850
R_free r_free	0.3190

Chicken Cytochrome BC1 Complex inhibited by an iodinated analogue of the polyketide Crocacin-D

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

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

MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, leader sequence

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

3cwb__assembly_1__model_1

3cwb__assembly_1__model_1 | I(q)

3cwb__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (21)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 polymer

Polymer Polymer

Entity 4 Entity 4 polymer

Polymer Polymer

Entity 5 Entity 5 polymer

Polymer Polymer

Entity 6 Entity 6 polymer

Polymer Polymer

Entity 7 Entity 7 polymer

Polymer Polymer

Entity 8 Entity 8 polymer

Polymer Polymer

Entity 9 Entity 9 polymer

Polymer Polymer

Entity 10 Entity 10 polymer

Polymer Polymer

Entity 11 Entity 11 non-polymer

Entity 12 Entity 12 non-polymer

Entity 13 Entity 13 non-polymer

Entity 14 Entity 14 non-polymer

Entity 15 Entity 15 non-polymer

Entity 16 Entity 16 non-polymer

Entity 17 Entity 17 non-polymer

Entity 18 Entity 18 non-polymer

Entity 19 Entity 19 non-polymer

Entity 20 Entity 20 non-polymer

Entity 21 Entity 21 water

6. Fold Classification (SCOP + CATH) 32 domains

SCOP 2.08 (4 domains)

CATH v4.4 (28 domains)

7. Citations (3)