7o3h

Murine CIII2 focus-refined from supercomplex CICIII2

Method: ELECTRON MICROSCOPY Dmax: 177.4 Å Quality: GOOD

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

Cytochrome b-c1 complex subunit 1, mitochondrial

OrganismNot specified

UniProt Q9CZ13

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain A; UniProt 35–480 Chain L; UniProt 35–480 Not recorded Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome b × 2 (P00158) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–446; UniProt 35–480 Author chain L; PDBConstruct 1–446; UniProt 35–480

Cytochrome b-c1 complex subunit 2, mitochondrial

OrganismNot specified

UniProt Q9DB77

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain B; UniProt 15–453 Chain M; UniProt 15–453 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b × 2 (P00158) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR2_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–439; UniProt 15–453 Author chain M; PDBConstruct 1–439; UniProt 15–453

Cytochrome b

OrganismNot specified

UniProt P00158

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain C; UniProt 1–381 Chain N; UniProt 1–381 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–381; UniProt 1–381 Author chain N; PDBConstruct 1–381; UniProt 1–381

Cytochrome c1, heme protein, mitochondrial

OrganismNot specified

UniProt Q9D0M3

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain D; UniProt 85–325 Chain O; UniProt 85–325 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome b × 2 (P00158) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CY1_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 85–325 Author chain O; PDBConstruct 1–241; UniProt 85–325

Cytochrome b-c1 complex subunit Rieske, mitochondrial

OrganismNot specified

UniProt Q9CR68

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain E; UniProt 79–274 Chain P; UniProt 79–274 Chain T; UniProt 1–78 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome b × 2 (P00158) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRI_MOUSE
Isoform
PDB entities 5, 11
Chains and sequence ranges Author chain E; PDBConstruct 1–196; UniProt 79–274 Author chain P; PDBConstruct 1–196; UniProt 79–274 Author chain T; PDBConstruct 1–78; UniProt 1–78

Cytochrome b-c1 complex subunit 7

OrganismNot specified

UniProt Q9CQB4

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain F; UniProt 2–111 Chain Q; UniProt 2–111 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome b × 2 (P00158) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q9CQB4_MOUSE
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–110; UniProt 2–111 Author chain Q; PDBConstruct 1–110; UniProt 2–111

Cytochrome b-c1 complex subunit 8

OrganismNot specified

UniProt Q9CQ69

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain G; UniProt 2–82 Chain R; UniProt 2–82 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome b × 2 (P00158) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR8_MOUSE
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–81; UniProt 2–82 Author chain R; PDBConstruct 1–81; UniProt 2–82

Cytochrome b-c1 complex subunit 6, mitochondrial

OrganismNot specified

UniProt P99028

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain H; UniProt 14–89 Chain S; UniProt 14–89 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome b × 2 (P00158) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR6_MOUSE
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–76; UniProt 14–89 Author chain S; PDBConstruct 1–76; UniProt 14–89

Cytochrome b-c1 complex subunit 9

OrganismNot specified

UniProt Q8R1I1

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain J; UniProt 2–64 Chain U; UniProt 2–64 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome b × 2 (P00158) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 10 × 2 (Q9CPX8) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR9_MOUSE
Isoform
PDB entities 9
Chains and sequence ranges Author chain J; PDBConstruct 1–63; UniProt 2–64 Author chain U; PDBConstruct 1–63; UniProt 2–64

Cytochrome b-c1 complex subunit 10

OrganismNot specified

UniProt Q9CPX8

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 × 21 PDB declaration: 21-meric(21) Consistent with protein copy count Chain K; UniProt 1–56 Chain V; UniProt 1–56 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (Q9CZ13) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (Q9DB77) Cytochrome b × 2 (P00158) Cytochrome c1, heme protein, mitochondrial × 2 (Q9D0M3) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q9CR68) Cytochrome b-c1 complex subunit 7 × 2 (Q9CQB4) Cytochrome b-c1 complex subunit 8 × 2 (Q9CQ69) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P99028) Cytochrome b-c1 complex subunit 9 × 2 (Q8R1I1) Cytochrome b-c1 complex subunit 9 × 1 (Q9CR68) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 8 CDL CARDIOLIPIN × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.7;CHAPS was added only upon freezing cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

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

View Construct and Data Evidence
UniProt name QCR10_MOUSE
Isoform
PDB entities 10
Chains and sequence ranges Author chain K; PDBConstruct 1–56; UniProt 1–56 Author chain V; 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 7o3h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7o3h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7o3h
Deposition date deposition_date2021-04-01
Structure title titleMurine CIII2 focus-refined from supercomplex CICIII2
Keywords keywordsmitochondria, respiratory chain, supercomplex, OXIDOREDUCTASE, complex III, complex IV, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.00
Radius of gyration Rg (electron density) rg_electron54.12
Forward intensity I(0) i03120270000.00
Molecular weight molecular_weight478900.0 kDa
Excluded volume excluded_volume603120 ų
Envelope volume envelope_volume847890 ų
Hydration-shell volume shell_volume126450 ų
Envelope diameter envelope_diameter175.9
Shell Rg shell_rg59.92
Envelope Rg envelope_rg53.12
Shape Rg shape_rg54.12
Total Rg total_rg54.28
Total atoms total_atoms33700
Residues n_residues4161
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 dmax177.4
Rg (real space) rg_real54.87
Rg uncertainty (real space) rg_real_error1.17
I(0) (real space) i0_real3.1200e+09
I(0) uncertainty (real space) i0_real_error5.9310e+07
Rg (reciprocal space) rg_reciprocal55.10
I(0) (reciprocal space) i0_reciprocal3121000000.0000
Solution quality estimate total_estimate0.8800
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.3
Skewness Skewness skewness0.236
Kurtosis Kurtosis kurtosis-0.538
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha366100000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.734

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7o3hA01
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_id7o3hA02
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_id7o3hE01
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_id7o3hL01
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_id7o3hL02
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_id7o3hP01
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

8. Citations (1)

9. Files and Curves (10)