5xte

Cryo-EM structure of human respiratory complex III (cytochrome bc1 complex)

Method: ELECTRON MICROSCOPY Dmax: 181.5 Å Quality: GOOD

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

Cytochrome b-c1 complex subunit 8

OrganismNot specified

UniProt O14949

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 2–82 Chain N; UniProt 2–82 Not recorded Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR8_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–81; UniProt 2–82 Author chain N; PDBConstruct 1–81; UniProt 2–82

Cytochrome b-c1 complex subunit Rieske, mitochondrial

OrganismNot specified

UniProt P47985

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain B; UniProt 1–57 Chain C; UniProt 79–274 Chain O; UniProt 1–57 Chain P; UniProt 79–274 Fragment:UNP RESIDUES 1-57 Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRI_HUMAN
Isoform
PDB entities 2, 3
Chains and sequence ranges Author chain B; PDBConstruct 1–57; UniProt 1–57 Author chain O; PDBConstruct 1–57; UniProt 1–57 Author chain C; PDBConstruct 1–196; UniProt 79–274 Author chain P; PDBConstruct 1–196; UniProt 79–274

Cytochrome b-c1 complex subunit 9

OrganismNot specified

UniProt Q9UDW1

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 2–63 Chain Q; UniProt 2–63 Not recorded Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR9_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–62; UniProt 2–63 Author chain Q; PDBConstruct 1–62; UniProt 2–63

Cytochrome b-c1 complex subunit 6, mitochondrial

OrganismNot specified

UniProt P07919

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 17–91 Chain R; UniProt 17–91 Not recorded Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR6_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–75; UniProt 17–91 Author chain R; PDBConstruct 1–75; UniProt 17–91

Cytochrome b-c1 complex subunit 7

OrganismNot specified

UniProt P14927

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 6–111 Chain S; UniProt 6–111 Fragment:UNP RESIDUES 6-111 Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR7_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–106; UniProt 6–111 Author chain S; PDBConstruct 1–106; UniProt 6–111

Cytochrome b-c1 complex subunit 10

OrganismNot specified

UniProt O14957

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 2–52 Chain T; UniProt 2–52 Fragment:UNP RESIDUES 2-52 Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR10_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–51; UniProt 2–52 Author chain T; PDBConstruct 1–51; UniProt 2–52

Cytochrome c1, heme protein, mitochondrial

OrganismNot specified

UniProt P08574

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 85–325 Chain U; UniProt 85–325 Not recorded Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CY1_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–241; UniProt 85–325 Author chain U; PDBConstruct 1–241; UniProt 85–325

Cytochrome b

OrganismNot specified

UniProt P00156

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 2–379 Chain V; UniProt 2–379 Not recorded Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CYB_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain J; PDBConstruct 1–378; UniProt 2–379 Author chain V; PDBConstruct 1–378; UniProt 2–379

Cytochrome b-c1 complex subunit 2, mitochondrial

OrganismNot specified

UniProt P22695

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 35–453 Chain W; UniProt 35–453 Fragment:UNP RESIDUES 35-453 Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31930) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR2_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain K; PDBConstruct 1–419; UniProt 35–453 Author chain W; PDBConstruct 1–419; UniProt 35–453

Cytochrome b-c1 complex subunit 1, mitochondrial

OrganismNot specified

UniProt P31930

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 L; UniProt 35–480 Chain Y; UniProt 35–480 Not recorded Cytochrome b-c1 complex subunit 8 × 2 (O14949) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (P47985) Cytochrome b-c1 complex subunit 9 × 2 (Q9UDW1) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P07919) Cytochrome b-c1 complex subunit 7 × 2 (P14927) Cytochrome b-c1 complex subunit 10 × 2 (O14957) Cytochrome c1, heme protein, mitochondrial × 2 (P08574) Cytochrome b × 2 (P00156) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P22695) CDL CARDIOLIPIN × 9 FES FE2/S2 (INORGANIC) CLUSTER × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 HEC HEME C × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-PHOSPHAOCTACOSANE-6,6,11-TRIOL × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name QCR1_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain L; PDBConstruct 1–446; UniProt 35–480 Author chain Y; PDBConstruct 1–446; UniProt 35–480

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 5xte

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5xte
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5xte
Deposition date deposition_date2017-06-19
Structure title titleCryo-EM structure of human respiratory complex III (cytochrome bc1 complex)
Keywords keywordsRespiratory, OXIDOREDUCTASE-ELECTRON TRANSPORT complex; OXIDOREDUCTASE/ELECTRON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.44
Radius of gyration Rg (electron density) rg_electron54.28
Forward intensity I(0) i03180370000.00
Molecular weight molecular_weight490030.0 kDa
Excluded volume excluded_volume619660 ų
Envelope volume envelope_volume869780 ų
Hydration-shell volume shell_volume128780 ų
Envelope diameter envelope_diameter179.2
Shell Rg shell_rg60.27
Envelope Rg envelope_rg53.48
Shape Rg shape_rg54.29
Total Rg total_rg54.38
Total atoms total_atoms34492
Residues n_residues4222
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 dmax181.5
Rg (real space) rg_real55.32
Rg uncertainty (real space) rg_real_error1.95
I(0) (real space) i0_real3.1800e+09
I(0) uncertainty (real space) i0_real_error6.4380e+07
Rg (reciprocal space) rg_reciprocal55.53
I(0) (reciprocal space) i0_reciprocal3181000000.0000
Solution quality estimate total_estimate0.8832
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary64.8
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha383300000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.818

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

7. Fold Classification (SCOP + CATH) 30 domains

CATH v4.4 (30 domains)

Domain ID domain_id5xteA00
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_id5xteB00
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_id5xteC01
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_id5xteC02
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_id5xteD00
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_id5xteE00
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_id5xteF00
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_id5xteG00
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
Domain ID domain_id5xteH01
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_id5xteH02
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_id5xteJ00
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_id5xteK01
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_id5xteK02
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_id5xteL01
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_id5xteL02
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_id5xteN00
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_id5xteO00
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_id5xteP01
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_id5xteP02
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_id5xteQ00
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_id5xteR00
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_id5xteS00
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_id5xteT00
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
Domain ID domain_id5xteU01
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_id5xteU02
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_id5xteV00
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_id5xteW01
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_id5xteW02
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_id5xteY01
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_id5xteY02
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

8. Citations (1)

9. Files and Curves (10)