3l72

Chicken cytochrome BC1 complex with kresoxim-I-dimethyl bound

Method: X-RAY DIFFRACTION

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

MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I

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 2 × 2 （D0VX29） CYTOCHROME B × 2 （P18946） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 （D0VX26） CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 （D0VX30） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 （D0VX32） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 （D0VX28） CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 （D0VX27） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D0VX31_CHICK
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–446； UniProt 1–446 Author chain N； PDBConstruct 1–446； UniProt 1–446

MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2

OrganismNot specified

UniProt D0VX29

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 （D0VX31） CYTOCHROME B × 2 （P18946） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 （D0VX26） CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 （D0VX30） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 （D0VX32） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 （D0VX28） CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 （D0VX27） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D0VX29_CHICK
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–441； UniProt 1–441 Author chain O； PDBConstruct 1–441； UniProt 1–441

CYTOCHROME B

OrganismNot specified

UniProt P18946

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 （D0VX31） MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 （D0VX29） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 （D0VX26） CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 （D0VX30） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 （D0VX32） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 （D0VX28） CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 （D0VX27） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	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 CYTOCHROME C1, HEME PROTEIN

OrganismNot specified

UniProt D0VX26

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 （D0VX31） MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 （D0VX29） CYTOCHROME B × 2 （P18946） CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 （D0VX30） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 （D0VX32） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 （D0VX28） CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 （D0VX27） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D0VX26_CHICK
Isoform	—
PDB entities	4
Chains and sequence ranges	Author chain D； PDBConstruct 1–241； UniProt 1–241 Author chain Q； PDBConstruct 1–241； UniProt 1–241

CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL

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 （D0VX31） MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 （D0VX29） CYTOCHROME B × 2 （P18946） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 （D0VX26） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 （D0VX30） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 （D0VX32） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 （D0VX28） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 （D0VX27） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	UCRI_CHICK
Isoform	—
PDB entities	5, 9
Chains and sequence ranges	Author chain E； PDBConstruct 1–196； UniProt 77–272 Author chain R； PDBConstruct 1–196； UniProt 77–272 Author chain I； PDBConstruct 16–47； UniProt 45–76 Author chain V； PDBConstruct 16–47； UniProt 45–76

MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN

OrganismNot specified

UniProt D0VX30

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 （D0VX31） MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 （D0VX29） CYTOCHROME B × 2 （P18946） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 （D0VX26） CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 （D0VX32） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 （D0VX28） CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 （D0VX27） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D0VX30_CHICK
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain F； PDBConstruct 1–110； UniProt 1–110 Author chain S； PDBConstruct 1–110； UniProt 1–110

MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C

OrganismNot specified

UniProt D0VX32

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 （D0VX31） MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 （D0VX29） CYTOCHROME B × 2 （P18946） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 （D0VX26） CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 （D0VX30） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 （D0VX28） CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 （D0VX27） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D0VX32_CHICK
Isoform	—
PDB entities	7
Chains and sequence ranges	Author chain G； PDBConstruct 1–81； UniProt 1–81 Author chain T； PDBConstruct 1–81； UniProt 1–81

MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII

OrganismNot specified

UniProt D0VX28

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 （D0VX31） MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 （D0VX29） CYTOCHROME B × 2 （P18946） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 （D0VX26） CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 （D0VX30） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 （D0VX32） CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN × 2 （D0VX27） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D0VX28_CHICK
Isoform	—
PDB entities	8
Chains and sequence ranges	Author chain H； PDBConstruct 1–77； UniProt 1–77 Author chain U； PDBConstruct 1–77； UniProt 1–77

MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN

OrganismNot specified

UniProt D0VX27

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 （D0VX31） MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2 × 2 （D0VX29） CYTOCHROME B × 2 （P18946） MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN × 2 （D0VX26） CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL × 2 （Q5ZLR5） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN × 2 （D0VX30） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C × 2 （D0VX32） MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII × 2 （D0VX28） CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL × 2 （Q5ZLR5） PROTOPORPHYRIN IX CONTAINING FE × 4 methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate × 2 Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 CARDIOLIPIN × 4 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 GLYCEROL × 2 HEME C × 2 octyl beta-D-glucopyranoside × 5 FE2/S2 (INORGANIC) CLUSTER × 2 water × 4	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	D0VX27_CHICK
Isoform	—
PDB entities	10
Chains and sequence ranges	Author chain J； PDBConstruct 1–61； UniProt 1–61 Author chain W； PDBConstruct 1–61； UniProt 1–61

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	3l72
Deposition date deposition_date	2009-12-27
Structure title title	Chicken cytochrome BC1 complex with kresoxim-I-dimethyl bound
Keywords keywords	;CYTOCHROME BC1, MEMBRANE PROTEIN, HEME PROTEIN, RIESKE IRON SULFUR PROTEIN, CYTOCHROME B, CYTOCHROME C1, COMPLEX III, MITOCHONDRIAL PROCESSING PROTEIN, UBIQUINONE, AZOXYSTROBIN OXIDOREDUCTASE, REDOX ENZYME RESPIRATORY CHAIN, ELECTRON TRANSPORT, HEME, INNER MEMBRANE, MEMBRANE, STROBILURINS BINDING, MITOCHONDRION, TRANSMEMBRANE, STIGMATELLIN, IRON, MITOCHONDRIAL INNER MEMBRANE, RESPIRATORY CHAIN, IRON-SULFUR, TRANSIT PEPTIDE, Metal-binding, Mitochondrion inner membrane, Transport, Disulfide bond, OXIDOREDUCTASE ;; 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.

3l72__assembly_1__model_1

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

Download this curve (.dat)

3l72__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3l72__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	55.35 Å
Rg (electron density)	54.44 Å
Total Rg	54.63 Å
Atom count	32627
Residues	4067
Excluded volume	583190 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3l72__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 (20)

Entity 1 Entity 1 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I
Molecular weight formula_weight	49503.8 kDa
EC 编号 ec_number	1.10.2.2
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	32648

AATYAQTLQNIPETNVTTLDNGLRVASEESSQPTCTVGVWIGAGSRYENEKNNGAGYFVEHLAFKGTKKRPCAAFEKEVESMGAHFNGYTSREQTAFYIKALSKDMPKVVELLADVVQNCALEESQIEKERGVILQELKEMDNDMTNVTFDYLHATAFQGTALARTVEGTTENIKHLTRADLASYIDTHFKAPRMVLAAAGGISHKELVDAARQHFSGVSFTYKEDAVPILPRCRFTGSEIRARDDALPVAHVALAVEGPGWADPDNVVLHVANAIIGRYDRTFGGGKHLSSRLAALAVEHKLCHSFQTFNTSYSDTGLFGFHFVADPLSIDDMMFCAQGEWMRLCTSTTESEVKRAKNHLRSAMVAQLDGTTPVCETIGSHLLNYGRRISLEEWDSRISAVDARMVRDVCSKYIYDKCPALAAVGPIEQLLDYNRIRSGMYWIRF

Entity 2 Entity 2 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2
Molecular weight formula_weight	46683.8 kDa
EC 编号 ec_number	1.10.2.2
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
EC 编号 ec_number	1.10.2.2
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
EC 编号 ec_number	1.10.2.2
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	CYTOCHROME B-C1 COMPLEX SUBUNIT 5, RIESKE IRONSULFUR PROTEIN, MITOCHONDRIAL
Molecular weight formula_weight	21506.2 kDa
EC 编号 ec_number	1.10.2.2
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	13394.4 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

AARATVAGGGRLMDRIRKWYYNAAGFNKYGLMRDDTLYEDDDVKEALKRLPEDLYNERMFRIKRALDLSLKHRILPKEQWVKYEEDKPYLEPYLKEVIRERLEREAWNKK

Entity 7 Entity 7 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE UBIQUINONE-BINDING PROTEIN QP-C
Molecular weight formula_weight	9498.7 kDa
EC 编号 ec_number	1.10.2.2
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
EC 编号 ec_number	1.10.2.2
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	CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL
Molecular weight formula_weight	4785.6 kDa
EC 编号 ec_number	1.10.2.2
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

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

XXXXXXXXXXXXXXXRPLLCRESMSGRSARRDLVAGISLNAPASVRY

Entity 10 Entity 10 polymer

Description description	MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 7.2 KDA PROTEIN
Molecular weight formula_weight	7006.0 kDa
EC 编号 ec_number	1.10.2.2
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	PROTOPORPHYRIN IX CONTAINING FE
Molecular weight formula_weight	616.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 12 Entity 12 non-polymer

Description description	methyl (2E)-{2-[(4-iodo-2,5-dimethylphenoxy)methyl]phenyl}(methoxyimino)ethanoate
Molecular weight formula_weight	453.3 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 13 Entity 13 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 14 Entity 14 non-polymer

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

Entity 15 Entity 15 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 16 Entity 16 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 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	octyl beta-D-glucopyranoside
Molecular weight formula_weight	292.4 kDa
Source method src_method	man
Copy count entity_count	5

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 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	18

▼

6. Fold Classification (SCOP + CATH) 56 domains

SCOP 2.08 (28 domains)

Domain ID domain_id	d3l72a1
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.185.1.0 — automated matches

Domain ID domain_id	d3l72a2
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.185.1.0 — automated matches

Domain ID domain_id	d3l72b1
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.185.1.0 — automated matches

Domain ID domain_id	d3l72b2
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.185.1.0 — automated matches

Domain ID domain_id	d3l72c1
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	d3l72c2
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	d3l72d1
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	d3l72d2
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	d3l72e1
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	d3l72e2
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	d3l72f_
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	d3l72g_
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	d3l72h_
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	d3l72j_
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	d3l72n1
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.185.1.0 — automated matches

Domain ID domain_id	d3l72n2
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.185.1.0 — automated matches

Domain ID domain_id	d3l72o1
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.185.1.0 — automated matches

Domain ID domain_id	d3l72o2
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.185.1.0 — automated matches

Domain ID domain_id	d3l72p1
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	d3l72p2
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	d3l72q1
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	d3l72q2
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	d3l72r1
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	d3l72r2
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	d3l72s_
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	d3l72t_
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	d3l72u_
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	d3l72w_
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)

CATH v4.4 (28 domains)

Domain ID domain_id	3l72A01
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	3l72A02
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	3l72B01
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	3l72B02
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	3l72C00
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	3l72D01
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	3l72D02
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	3l72E01
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	3l72E02
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	3l72F00
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	3l72G00
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	3l72H00
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	3l72I00
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	3l72J00
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	3l72N01
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	3l72N02
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	3l72O01
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	3l72O02
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	3l72P00
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	3l72Q01
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	3l72Q02
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	3l72R01
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	3l72R02
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	3l72S00
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	3l72T00
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	3l72U00
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	3l72V00
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	3l72W00
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

▶

Unit-cell length a length_a	172.614 Å
Unit-cell length b length_b	181.548 Å
Unit-cell length c length_c	241.033 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	3.060 Å
Low-resolution limit resolution_low	28.930 Å
R factor r_factor	0.2640
R_work r_work	0.2640
R_free r_free	0.2940

Chicken cytochrome BC1 complex with kresoxim-I-dimethyl bound

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

MITOCHONDRIAL UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I

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 COMPLEX CORE PROTEIN 2

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

MITOCHONDRIAL CYTOCHROME C1, HEME PROTEIN

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 5, RIESKE IRONSULFUR 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

MITOCHONDRIAL UBIQUINOL-CYTOCHROME C REDUCTASE 14 KDA PROTEIN

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 UBIQUINONE-BINDING PROTEIN QP-C

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 11 KDA PROTEIN, COMPLEX III SUBUNIT VIII

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 7.2 KDA PROTEIN

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

3l72__assembly_1__model_1

3l72__assembly_1__model_1 | I(q)

3l72__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment