6fo0

CryoEM structure of bovine cytochrome bc1 in complex with the anti-malarial compound GSK932121

Method: ELECTRON MICROSCOPY Dmax: 157.3 Å Quality: REASONABLE

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

Cytochrome b-c1 complex subunit 1, 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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain A; UniProt 1–480 Chain N; UniProt 1–480 Not recorded Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Chain I/V × 2 Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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 QCR1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–480; UniProt 1–480 Author chain N; PDBConstruct 1–480; UniProt 1–480

Cytochrome b-c1 complex subunit 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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain B; UniProt 1–453 Chain O; UniProt 1–453 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Chain I/V × 2 Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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 QCR2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–453; UniProt 1–453 Author chain O; 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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain C; UniProt 1–379 Chain P; UniProt 1–379 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Chain I/V × 2 Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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 Author chain P; 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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain D; UniProt 1–325 Chain Q; UniProt 1–325 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Chain I/V × 2 Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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 1–325; UniProt 1–325 Author chain Q; PDBConstruct 1–325; UniProt 1–325

Cytochrome b-c1 complex subunit Rieske, 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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain E; UniProt 1–274 Chain R; UniProt 1–274 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Chain I/V × 2 Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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
Chains and sequence ranges Author chain E; PDBConstruct 1–274; UniProt 1–274 Author chain R; PDBConstruct 1–274; UniProt 1–274

Cytochrome b-c1 complex subunit 7

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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain F; UniProt 1–111 Chain S; UniProt 1–111 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Chain I/V × 2 Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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 QCR7_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–111; UniProt 1–111 Author chain S; PDBConstruct 1–111; UniProt 1–111

Cytochrome b-c1 complex subunit 8

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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain G; UniProt 1–82 Chain T; UniProt 1–82 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Chain I/V × 2 Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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 QCR8_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–82; UniProt 1–82 Author chain T; PDBConstruct 1–82; UniProt 1–82

Cytochrome b-c1 complex subunit 6, mitochondrial

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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain H; UniProt 1–91 Chain U; UniProt 1–91 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Chain I/V × 2 Cytochrome b-c1 complex subunit 9 × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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 QCR6_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–91; UniProt 1–91 Author chain U; PDBConstruct 1–91; UniProt 1–91

Cytochrome b-c1 complex subunit 9

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 × 20 PDB declaration: eicosameric(20) Consistent with protein copy count Chain J; UniProt 1–64 Chain W; UniProt 1–64 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Chain I/V × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 G8U 3-chloro-6-(hydroxymethyl)-2-methyl-5-{4-[3-(trifluoromethoxy)phenoxy]phenyl}pyridin-4-ol × 2 HEC HEME C × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 6 seconds with a blot force of 6 before plunge-freezing Resolution 4.10 Å

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 QCR9_BOVIN
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–64; UniProt 1–64 Author chain W; PDBConstruct 1–64; UniProt 1–64

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 6fo0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6fo0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6fo0
Deposition date deposition_date2018-02-05
Structure title titleCryoEM structure of bovine cytochrome bc1 in complex with the anti-malarial compound GSK932121
Keywords keywordsCryo-EM, Inhibitor binding, Membrane protein, cytochrome bc1; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.17
Radius of gyration Rg (electron density) rg_electron54.29
Forward intensity I(0) i02659400000.00
Molecular weight molecular_weight439980.0 kDa
Excluded volume excluded_volume553230 ų
Envelope volume envelope_volume806820 ų
Hydration-shell volume shell_volume120190 ų
Envelope diameter envelope_diameter170.0
Shell Rg shell_rg59.84
Envelope Rg envelope_rg53.19
Shape Rg shape_rg54.27
Total Rg total_rg54.51
Total atoms total_atoms61354
Residues n_residues3908
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 dmax157.3
Rg (real space) rg_real55.03
Rg uncertainty (real space) rg_real_error0.93
I(0) (real space) i0_real2.6590e+09
I(0) uncertainty (real space) i0_real_error4.8430e+07
Rg (reciprocal space) rg_reciprocal55.26
I(0) (reciprocal space) i0_reciprocal2660000000.0000
Solution quality estimate total_estimate0.6153
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.1
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.586
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha271500000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.998; Stabil: 1.000; Sysdev: 0.001; Positv: 1.000; Valcen: 0.996; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)