1sqp

Crystal Structure Analysis of Bovine Bc1 with Myxothiazol

Method: X-RAY DIFFRACTION Dmax: 166.4 Å Quality: GOOD

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

Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor

OrganismNot specified

UniProt P31800

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain A; UniProt 1–480 Fragment:core protein 1 Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) sub6 × 2 Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C × 2 (P13271) Ubiquinol-cytochrome c reductase complex 11 kDa protein × 2 (P00126) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) Ubiquinol-cytochrome c reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome c reductase complex 6.4 kDa protein × 2 (P07552) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

46 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UQCR1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–480; UniProt 1–480

Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor

OrganismNot specified

UniProt P23004

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain B; UniProt 1–453 Fragment:core protein 2 Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor × 2 (P31800) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) sub6 × 2 Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C × 2 (P13271) Ubiquinol-cytochrome c reductase complex 11 kDa protein × 2 (P00126) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) Ubiquinol-cytochrome c reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome c reductase complex 6.4 kDa protein × 2 (P07552) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UQCR2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–453; UniProt 1–453

Cytochrome b

OrganismNot specified

UniProt P00157

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain C; UniProt 1–379 Fragment:cytochrome b Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor × 2 (P31800) Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor × 2 (P23004) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) sub6 × 2 Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C × 2 (P13271) Ubiquinol-cytochrome c reductase complex 11 kDa protein × 2 (P00126) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) Ubiquinol-cytochrome c reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome c reductase complex 6.4 kDa protein × 2 (P07552) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

45 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–379; UniProt 1–379

Cytochrome c1, heme protein, mitochondrial

OrganismNot specified

UniProt P00125

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain D; UniProt 1–241 Fragment:cytochrome c1 Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor × 2 (P31800) Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor × 2 (P23004) Cytochrome b × 2 (P00157) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) sub6 × 2 Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C × 2 (P13271) Ubiquinol-cytochrome c reductase complex 11 kDa protein × 2 (P00126) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) Ubiquinol-cytochrome c reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome c reductase complex 6.4 kDa protein × 2 (P07552) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CY1_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 1–241

;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ;

OrganismNot specified

UniProt P13272

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain E; UniProt 79–274 Chain I; UniProt 1–78 Fragment:iron sulfur protein Fragment:subunit 9 Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor × 2 (P31800) Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) sub6 × 2 Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C × 2 (P13271) Ubiquinol-cytochrome c reductase complex 11 kDa protein × 2 (P00126) Ubiquinol-cytochrome c reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome c reductase complex 6.4 kDa protein × 2 (P07552) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

48 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRI_BOVIN
Isoform
PDB entities 5, 9
Chains and sequence ranges Author chain E; PDBConstruct 1–196; UniProt 79–274 Author chain I; PDBConstruct 1–78; UniProt 1–78

Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C

OrganismNot specified

UniProt P13271

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain G; UniProt 1–81 Fragment:subunit 7 Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor × 2 (P31800) Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) sub6 × 2 Ubiquinol-cytochrome c reductase complex 11 kDa protein × 2 (P00126) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) Ubiquinol-cytochrome c reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome c reductase complex 6.4 kDa protein × 2 (P07552) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRQ_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–81; UniProt 1–81

Ubiquinol-cytochrome c reductase complex 11 kDa protein

OrganismNot specified

UniProt P00126

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain H; UniProt 1–78 Fragment:subunit 8 Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor × 2 (P31800) Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) sub6 × 2 Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C × 2 (P13271) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) Ubiquinol-cytochrome c reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome c reductase complex 6.4 kDa protein × 2 (P07552) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

46 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRH_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–78; UniProt 1–78

Ubiquinol-cytochrome c reductase complex 7.2 kDa protein

OrganismNot specified

UniProt P00130

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain J; UniProt 1–62 Fragment:subunit 10 Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor × 2 (P31800) Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) sub6 × 2 Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C × 2 (P13271) Ubiquinol-cytochrome c reductase complex 11 kDa protein × 2 (P00126) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) Ubiquinol-cytochrome c reductase complex 6.4 kDa protein × 2 (P07552) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCR10_BOVIN
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–62; UniProt 1–62

Ubiquinol-cytochrome c reductase complex 6.4 kDa protein

OrganismNot specified

UniProt P07552

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain K; UniProt 1–56 Fragment:subunit 11 Ubiquinol-cytochrome-c reductase complex core protein I, mitochondrial precursor × 2 (P31800) Ubiquinol-cytochrome-c reductase complex core protein 2, mitochondrial precursor × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) sub6 × 2 Ubiquinol-cytochrome c reductase complex ubiquinone-binding protein QP-C × 2 (P13271) Ubiquinol-cytochrome c reductase complex 11 kDa protein × 2 (P00126) ;Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial precursor (EC 1.10.2.2) (Rieske iron-sulfur protein) (RISP) [Contains: Ubiquinol-cytochrome c reductase 8 kDa protein (Complex III subunit IX)] ; × 2 (P13272) Ubiquinol-cytochrome c reductase complex 7.2 kDa protein × 2 (P00130) CDL CARDIOLIPIN × 6 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 6 MYX (2Z,6E)-7-{2'-[(2E,4E)-1,6-DIMETHYLHEPTA-2,4-DIENYL]-2,4'-BI-1,3-THIAZOL-4-YL}-3,5-DIMETHOXY-4-METHYLHEPTA-2,6-DIENAMID E × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 2.70 Å R-free 0.314

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.

29 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCR11_BOVIN
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–56; UniProt 1–56

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 1sqp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1sqp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1sqp
Deposition date deposition_date2004-03-19
Structure title titleCrystal Structure Analysis of Bovine Bc1 with Myxothiazol
Keywords keywordscytochrome bc1, Qo inhibitor, membrane protein, electron transport, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier49.08
Radius of gyration Rg (electron density) rg_electron48.68
Forward intensity I(0) i0807949000.00
Molecular weight molecular_weight242400.0 kDa
Excluded volume excluded_volume306040 ų
Envelope volume envelope_volume429370 ų
Hydration-shell volume shell_volume74755 ų
Envelope diameter envelope_diameter164.2
Shell Rg shell_rg50.73
Envelope Rg envelope_rg48.61
Shape Rg shape_rg48.70
Total Rg total_rg48.70
Total atoms total_atoms17059
Residues n_residues2102
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 dmax166.4
Rg (real space) rg_real49.42
Rg uncertainty (real space) rg_real_error1.68
I(0) (real space) i0_real8.0790e+08
I(0) uncertainty (real space) i0_real_error1.6190e+07
Rg (reciprocal space) rg_reciprocal49.08
I(0) (reciprocal space) i0_reciprocal807600000.0000
Solution quality estimate total_estimate0.8501
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.8
Skewness Skewness skewness0.421
Kurtosis Kurtosis kurtosis-0.571
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86730000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.813; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.922; Smooth: 0.686

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

7. Fold Classification (SCOP + CATH) 31 domains

SCOP 2.08 (16 domains)

Domain ID domain_idd1sqpa1
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.185.1.1 — MPP-like
Domain ID domain_idd1sqpa2
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.185.1.1 — MPP-like
Domain ID domain_idd1sqpb1
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.185.1.1 — MPP-like
Domain ID domain_idd1sqpb2
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.185.1.1 — MPP-like
Domain ID domain_idd1sqpc1
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_idd1sqpc2
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_idd1sqpd1
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_idd1sqpd2
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.23.11.1 — Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor
Domain ID domain_idd1sqpe1
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.23.12.1 — ISP transmembrane anchor
Domain ID domain_idd1sqpe2
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_idd1sqpf1
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_idd1sqpg_
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_idd1sqph_
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_idd1sqpi_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.184 — Non-globular alpha+beta subunits of globular proteins
Superfamily Superfamily superfamilyd.184.1 — Non-globular alpha+beta subunits of globular proteins
Family Family familyd.184.1.3 — Ubiquinol-cytochrome c reductase 8 kDa protein
Domain ID domain_idd1sqpj_
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_idd1sqpk1
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.15 — Subunit XI (6.4 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.23.15.1 — Subunit XI (6.4 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

CATH v4.4 (15 domains)

Domain ID domain_id1sqpA01
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_id1sqpA02
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_id1sqpB01
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_id1sqpB02
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_id1sqpC00
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_id1sqpD01
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_id1sqpD02
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_id1sqpE01
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_id1sqpE02
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_id1sqpF00
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_id1sqpG00
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_id1sqpH00
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_id1sqpI00
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_id1sqpJ00
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_id1sqpK00
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 superfamily220

8. Citations (3)

9. Files and Curves (10)