8iar

Respiratory complex CIII2, focus-refined of type I, Wild type mouse under thermoneutral temperature

Method: ELECTRON MICROSCOPY Dmax: 176.6 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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AA; UniProt 1–480 Chain Aa; UniProt 1–480 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AA; PDBConstruct 1–480; UniProt 1–480 Author chain Aa; PDBConstruct 1–480; UniProt 1–480

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AB; UniProt 1–453 Chain Ab; UniProt 1–453 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AB; PDBConstruct 1–453; UniProt 1–453 Author chain Ab; PDBConstruct 1–453; UniProt 1–453

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AC; UniProt 1–381 Chain Ac; 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AC; PDBConstruct 1–381; UniProt 1–381 Author chain Ac; 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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AD; UniProt 1–325 Chain Ad; UniProt 1–325 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AD; PDBConstruct 1–325; UniProt 1–325 Author chain Ad; PDBConstruct 1–325; UniProt 1–325

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AE; UniProt 1–274 Chain AI; UniProt 1–274 Chain Ae; UniProt 1–274 Chain Ai; UniProt 1–274 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 × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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
Chains and sequence ranges Author chain AE; PDBConstruct 1–274; UniProt 1–274 Author chain AI; PDBConstruct 1–274; UniProt 1–274 Author chain Ae; PDBConstruct 1–274; UniProt 1–274 Author chain Ai; PDBConstruct 1–274; UniProt 1–274

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AF; UniProt 1–111 Chain Af; UniProt 1–111 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AF; PDBConstruct 1–111; UniProt 1–111 Author chain Af; PDBConstruct 1–111; UniProt 1–111

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AG; UniProt 1–82 Chain Ag; UniProt 1–82 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AG; PDBConstruct 1–82; UniProt 1–82 Author chain Ag; PDBConstruct 1–82; UniProt 1–82

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AH; UniProt 1–89 Chain Ah; UniProt 1–89 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AH; PDBConstruct 1–89; UniProt 1–89 Author chain Ah; PDBConstruct 1–89; UniProt 1–89

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AJ; UniProt 1–64 Chain Aj; UniProt 1–64 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AJ; PDBConstruct 1–64; UniProt 1–64 Author chain Aj; PDBConstruct 1–64; UniProt 1–64

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain AK; UniProt 1–56 Chain Ak; 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 × 4 (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) 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 6 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 U10 UBIQUINONE-10 × 2 UQ6 5-(3,7,11,15,19,23-HEXAMETHYL-TETRACOSA-2,6,10,14,18,22-HEXAENYL)-2,3-DIMETHOXY-6-METHYL-BENZENE-1,4-DIOL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 5 PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 AK; PDBConstruct 1–56; UniProt 1–56 Author chain Ak; 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 8iar

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8iar
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8iar
Deposition date deposition_date2023-02-09
Structure title titleRespiratory complex CIII2, focus-refined of type I, Wild type mouse under thermoneutral temperature
Keywords keywordsRespiratory complex, Respiratory supercomplex, ELECTRON TRANSPORT; ELECTRON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier54.33
Radius of gyration Rg (electron density) rg_electron53.40
Forward intensity I(0) i02821900000.00
Molecular weight molecular_weight457860.0 kDa
Excluded volume excluded_volume577750 ų
Envelope volume envelope_volume795280 ų
Hydration-shell volume shell_volume121110 ų
Envelope diameter envelope_diameter173.8
Shell Rg shell_rg58.76
Envelope Rg envelope_rg52.15
Shape Rg shape_rg53.39
Total Rg total_rg53.56
Total atoms total_atoms32253
Residues n_residues3976
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax176.6
Rg (real space) rg_real54.19
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real2.8220e+09
I(0) uncertainty (real space) i0_real_error5.7730e+07
Rg (reciprocal space) rg_reciprocal54.42
I(0) (reciprocal space) i0_reciprocal2823000000.0000
Solution quality estimate total_estimate0.8855
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary67.0
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha257400000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.825

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

8. Citations (1)

9. Files and Curves (10)