3l71

Cytochrome BC1 complex from chicken with azoxystrobin bound

Method: X-RAY DIFFRACTION Dmax: 176.6 Å Quality: GOOD

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

Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i

OrganismNot specified

UniProt D0VX31

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain A; UniProt 1–446 Chain N; UniProt 1–446 Not recorded 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 Rieske, 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain B; UniProt 1–441 Chain O; UniProt 1–441 Not recorded 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 Rieske, 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain C; UniProt 1–380 Chain P; UniProt 1–380 Not recorded 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 Rieske, 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain D; UniProt 1–241 Chain Q; UniProt 1–241 Not recorded 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 Rieske, 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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 Rieske, mitochondrial

OrganismNot specified

UniProt Q5ZLR5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain E; UniProt 77–272 Chain I; UniProt 45–76 Chain R; UniProt 77–272 Chain V; UniProt 45–76 Fragment:UNP RESIDUES 77-272 Fragment:UNP RESIDUES 45-76 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain F; UniProt 1–110 Chain S; UniProt 1–110 Not recorded 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 Rieske, 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain G; UniProt 1–81 Chain T; UniProt 1–81 Not recorded 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 Rieske, 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain H; UniProt 1–77 Chain U; UniProt 1–77 Not recorded 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 Rieske, 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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 Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain J; UniProt 1–61 Chain W; UniProt 1–61 Not recorded 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 Rieske, 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) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZO METHYL (2Z)-2-(2-{[6-(2-CYANOPHENOXY)PYRIMIDIN-4-YL]OXY}PHENYL)-3-METHOXYACRYLATE × 2 UQ Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer × 2 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 5 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;277 K;FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.84 Å R-free 0.281

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

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.

SAXS scattering curve SAXS Profile

SAXS profile for 3l71

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3l71
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3l71
Deposition date deposition_date2009-12-27
Structure title titleCytochrome BC1 complex from chicken with azoxystrobin 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 methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier55.35
Radius of gyration Rg (electron density) rg_electron54.42
Forward intensity I(0) i02949530000.00
Molecular weight molecular_weight463800.0 kDa
Excluded volume excluded_volume583170 ų
Envelope volume envelope_volume809810 ų
Hydration-shell volume shell_volume120220 ų
Envelope diameter envelope_diameter177.8
Shell Rg shell_rg59.81
Envelope Rg envelope_rg53.51
Shape Rg shape_rg54.39
Total Rg total_rg54.63
Total atoms total_atoms32633
Residues n_residues4066
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax176.6
Rg (real space) rg_real55.22
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real2.9500e+09
I(0) uncertainty (real space) i0_real_error5.5870e+07
Rg (reciprocal space) rg_reciprocal55.44
I(0) (reciprocal space) i0_reciprocal2950000000.0000
Solution quality estimate total_estimate0.8721
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.1
Skewness Skewness skewness0.221
Kurtosis Kurtosis kurtosis-0.572
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha274100000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.931; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.552

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (20)

7. Fold Classification (SCOP + CATH) 56 domains

SCOP 2.08 (28 domains)

Domain ID domain_idd3l71a1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.0 — automated matches
Domain ID domain_idd3l71a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.0 — automated matches
Domain ID domain_idd3l71b1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.0 — automated matches
Domain ID domain_idd3l71b2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.0 — automated matches
Domain ID domain_idd3l71c1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.21 — Heme-binding four-helical bundle
Superfamily Superfamily superfamilyf.21.1 — Transmembrane di-heme cytochromes
Family Family familyf.21.1.2 — Cytochrome b of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71c2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.32 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.32.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.32.1.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71d1
Class classa — All alpha proteins
Fold Fold folda.3 — Cytochrome c
Superfamily Superfamily superfamilya.3.1 — Cytochrome c
Family Family familya.3.1.3 — Cytochrome bc1 domain
Domain ID domain_idd3l71d2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.11 — Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor
Family Family familyf.23.11.0 — automated matches
Domain ID domain_idd3l71e1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.12 — ISP transmembrane anchor
Family Family familyf.23.12.0 — automated matches
Domain ID domain_idd3l71e2
Class classb — All beta proteins
Fold Fold foldb.33 — ISP domain
Superfamily Superfamily superfamilyb.33.1 — ISP domain
Family Family familyb.33.1.1 — Rieske iron-sulfur protein (ISP)
Domain ID domain_idd3l71f_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.27 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.27.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.27.1.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71g_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.13 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.23.13.1 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71h_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.28 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.28.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.28.1.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71j_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.14 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.23.14.1 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71n1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.0 — automated matches
Domain ID domain_idd3l71n2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.0 — automated matches
Domain ID domain_idd3l71o1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.0 — automated matches
Domain ID domain_idd3l71o2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.0 — automated matches
Domain ID domain_idd3l71p1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.21 — Heme-binding four-helical bundle
Superfamily Superfamily superfamilyf.21.1 — Transmembrane di-heme cytochromes
Family Family familyf.21.1.2 — Cytochrome b of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71p2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.32 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.32.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.32.1.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71q1
Class classa — All alpha proteins
Fold Fold folda.3 — Cytochrome c
Superfamily Superfamily superfamilya.3.1 — Cytochrome c
Family Family familya.3.1.3 — Cytochrome bc1 domain
Domain ID domain_idd3l71q2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.11 — Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor
Family Family familyf.23.11.0 — automated matches
Domain ID domain_idd3l71r1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.12 — ISP transmembrane anchor
Family Family familyf.23.12.0 — automated matches
Domain ID domain_idd3l71r2
Class classb — All beta proteins
Fold Fold foldb.33 — ISP domain
Superfamily Superfamily superfamilyb.33.1 — ISP domain
Family Family familyb.33.1.1 — Rieske iron-sulfur protein (ISP)
Domain ID domain_idd3l71s_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.27 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.27.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.27.1.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71t_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.13 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.23.13.1 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71u_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.28 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.28.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.28.1.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3l71w_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.14 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.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_id3l71A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id3l71A02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id3l71B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id3l71B02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id3l71C00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology810 — Cytochrome Bc1 Complex; Chain C
Homologous superfamily homologous superfamily10 — Cytochrome Bc1 Complex; Chain C
Domain ID domain_id3l71D01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain
Domain ID domain_id3l71D02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily100 — Cytochrome c1, transmembrane anchor, C-terminal
Domain ID domain_id3l71E01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily270 — Ubiquinol cytochrome reductase, transmembrane domain
Domain ID domain_id3l71E02
Class class2 — Mainly Beta
Architecture architecture102 — 3-layer Sandwich
Topology topology10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily10 — Rieske [2Fe-2S] iron-sulphur domain
Domain ID domain_id3l71F00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1090 — Cytochrome Bc1 Complex; Chain F
Homologous superfamily homologous superfamily10 — Cytochrome b-c1 complex subunit 7
Domain ID domain_id3l71G00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily210 — Cytochrome b-c1 complex subunit 8
Domain ID domain_id3l71H00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily20 — Ubiquinol-cytochrome C reductase hinge domain
Domain ID domain_id3l71I00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology210 — Cytochrome Bc1 Complex; Chain I
Homologous superfamily homologous superfamily10 — Cytochrome Bc1 Complex; Chain I
Domain ID domain_id3l71J00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily260 — Cytochrome b-c1 complex subunit 9
Domain ID domain_id3l71N01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id3l71N02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id3l71O01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id3l71O02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology830 — Cytochrome Bc1 Complex; Chain A, domain 1
Homologous superfamily homologous superfamily10 — Metalloenzyme, LuxS/M16 peptidase-like
Domain ID domain_id3l71P00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology810 — Cytochrome Bc1 Complex; Chain C
Homologous superfamily homologous superfamily10 — Cytochrome Bc1 Complex; Chain C
Domain ID domain_id3l71Q01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology760 — Cytochrome Bc1 Complex; Chain D, domain 2
Homologous superfamily homologous superfamily10 — Cytochrome c-like domain
Domain ID domain_id3l71Q02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily100 — Cytochrome c1, transmembrane anchor, C-terminal
Domain ID domain_id3l71R01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily270 — Ubiquinol cytochrome reductase, transmembrane domain
Domain ID domain_id3l71R02
Class class2 — Mainly Beta
Architecture architecture102 — 3-layer Sandwich
Topology topology10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily10 — Rieske [2Fe-2S] iron-sulphur domain
Domain ID domain_id3l71S00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology1090 — Cytochrome Bc1 Complex; Chain F
Homologous superfamily homologous superfamily10 — Cytochrome b-c1 complex subunit 7
Domain ID domain_id3l71T00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily210 — Cytochrome b-c1 complex subunit 8
Domain ID domain_id3l71U00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily20 — Ubiquinol-cytochrome C reductase hinge domain
Domain ID domain_id3l71V00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology210 — Cytochrome Bc1 Complex; Chain I
Homologous superfamily homologous superfamily10 — Cytochrome Bc1 Complex; Chain I
Domain ID domain_id3l71W00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily260 — Cytochrome b-c1 complex subunit 9

8. Citations (1)

9. Files and Curves (10)