1nu1

Crystal Structure of Mitochondrial Cytochrome bc1 Complexed with 2-nonyl-4-hydroxyquinoline N-oxide (NQNO)

Method: X-RAY DIFFRACTION Dmax: 171.3 Å Quality: GOOD

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

Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial

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 35–480 Not recorded Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) cytochrome c1 × 2 (P00125) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) 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 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome C reductase complex 6.4 kDa protein × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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 1–446; UniProt 35–480

Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial

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 15–453 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Cytochrome b × 2 (P00157) cytochrome c1 × 2 (P00125) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) 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 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome C reductase complex 6.4 kDa protein × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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 1–439; UniProt 15–453

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 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) cytochrome c1 × 2 (P00125) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) 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 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome C reductase complex 6.4 kDa protein × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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

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 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) 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 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome C reductase complex 6.4 kDa protein × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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

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 1–57 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) cytochrome c1 × 2 (P00125) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) 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) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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 1–57; UniProt 1–57

Ubiquinol-cytochrome C reductase complex 14 kDa protein

OrganismNot specified

UniProt P00129

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 F; UniProt 1–110 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) cytochrome c1 × 2 (P00125) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) 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 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome C reductase complex 6.4 kDa protein × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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 UCR6_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–110; UniProt 1–110

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 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) cytochrome c1 × 2 (P00125) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) Ubiquinol-cytochrome C reductase complex 11 kDa protein × 2 (P00126) Ubiquinol-cytochrome C reductase 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome C reductase complex 6.4 kDa protein × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) cytochrome c1 × 2 (P00125) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein QP-C × 2 (P13271) Ubiquinol-cytochrome C reductase 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 7.2 kDa protein × 2 (P00130) Ubiquinol-cytochrome C reductase complex 6.4 kDa protein × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) cytochrome c1 × 2 (P00125) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) 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 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 6.4 kDa protein × 2 (P07552) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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 Not recorded Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial × 2 (P31800) Ubiquinol-cytochrome C reductase complex core protein 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) cytochrome c1 × 2 (P00125) UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial × 2 (P13272) Ubiquinol-cytochrome C reductase complex 14 kDa protein × 2 (P00129) 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 8 kDa protein × 2 (P13272) Ubiquinol-cytochrome C reductase complex 7.2 kDa protein × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 QNO 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 7.2;277 K;PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K Resolution 3.20 Å R-free 0.296

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 1nu1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1nu1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1nu1
Deposition date deposition_date2003-01-30
Structure title titleCrystal Structure of Mitochondrial Cytochrome bc1 Complexed with 2-nonyl-4-hydroxyquinoline N-oxide (NQNO)
Keywords keywords;BC1, QCR, MEMBRANE PROTEIN, PROTON TRANSLOCATION, ELECTRON TRANSFER, PROTEASE, MPP, MITOCHONDRIAL PROCESSING PEPTIDASE, CYTOCHROME C1, CYTOCHROME B, RIESKE, IRON SULFUR PROTEIN, OXIDOREDUCTASE, 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE (NQNO) ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier49.42
Radius of gyration Rg (electron density) rg_electron49.18
Forward intensity I(0) i0787907000.00
Molecular weight molecular_weight236520.0 kDa
Excluded volume excluded_volume297370 ų
Envelope volume envelope_volume424340 ų
Hydration-shell volume shell_volume73348 ų
Envelope diameter envelope_diameter166.1
Shell Rg shell_rg51.07
Envelope Rg envelope_rg48.86
Shape Rg shape_rg49.18
Total Rg total_rg49.29
Total atoms total_atoms16664
Residues n_residues2105
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 dmax171.3
Rg (real space) rg_real49.76
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real7.8790e+08
I(0) uncertainty (real space) i0_real_error1.5210e+07
Rg (reciprocal space) rg_reciprocal49.42
I(0) (reciprocal space) i0_reciprocal787600000.0000
Solution quality estimate total_estimate0.7878
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.2
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.594
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85190000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.900; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

7. Fold Classification (SCOP + CATH) 31 domains

SCOP 2.08 (16 domains)

Domain ID domain_idd1nu1a1
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_idd1nu1a2
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_idd1nu1b1
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_idd1nu1b2
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_idd1nu1c1
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_idd1nu1c2
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_idd1nu1d1
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_idd1nu1d2
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_idd1nu1e1
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_idd1nu1e2
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_idd1nu1f_
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_idd1nu1g_
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_idd1nu1h_
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_idd1nu1i_
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_idd1nu1j_
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_idd1nu1k_
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_id1nu1A01
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_id1nu1A02
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_id1nu1B01
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_id1nu1B02
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_id1nu1C00
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_id1nu1D01
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_id1nu1D02
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_id1nu1E01
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_id1nu1E02
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_id1nu1F00
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_id1nu1G00
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_id1nu1H00
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_id1nu1I00
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_id1nu1J00
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_id1nu1K00
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

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