4u3f

Cytochrome bc1 complex from chicken with designed inhibitor bound

Method: X-RAY DIFFRACTION Dmax: 175.9 Å Quality: GOOD

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

Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i

OrganismNot specified

UniProt D0VX31

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 1–446 Chain N; UniProt 1–446 Not recorded Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 × 2 (D0VX29) Cytochrome b × 2 (P18946) Mitochondrial cytochrome c1, heme protein × 2 (D0VX26) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Cytochrome b-c1 complex subunit 7 × 2 (D0VX30) Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c × 2 (D0VX32) Cytochrome b-c1 complex subunit 6 × 2 (D0VX28) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein × 2 (D0VX27) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0VX31_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–446; UniProt 1–446 Author chain N; PDBConstruct 1–446; UniProt 1–446

Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2

OrganismNot specified

UniProt D0VX29

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 1–441 Chain O; UniProt 1–441 Not recorded Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i × 2 (D0VX31) Cytochrome b × 2 (P18946) Mitochondrial cytochrome c1, heme protein × 2 (D0VX26) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Cytochrome b-c1 complex subunit 7 × 2 (D0VX30) Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c × 2 (D0VX32) Cytochrome b-c1 complex subunit 6 × 2 (D0VX28) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein × 2 (D0VX27) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0VX29_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–441; UniProt 1–441 Author chain O; PDBConstruct 1–441; UniProt 1–441

Cytochrome b

OrganismNot specified

UniProt P18946

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 2–380 Chain P; UniProt 2–380 Non-standard monomer:Yes (specific site not provided by mmCIF) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i × 2 (D0VX31) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 × 2 (D0VX29) Mitochondrial cytochrome c1, heme protein × 2 (D0VX26) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Cytochrome b-c1 complex subunit 7 × 2 (D0VX30) Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c × 2 (D0VX32) Cytochrome b-c1 complex subunit 6 × 2 (D0VX28) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein × 2 (D0VX27) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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 CYB_CHICK
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 2–380; UniProt 2–380 Author chain P; PDBConstruct 2–380; UniProt 2–380

Mitochondrial cytochrome c1, heme protein

OrganismNot specified

UniProt D0VX26

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 1–241 Chain Q; UniProt 1–241 Not recorded Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i × 2 (D0VX31) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 × 2 (D0VX29) Cytochrome b × 2 (P18946) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Cytochrome b-c1 complex subunit 7 × 2 (D0VX30) Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c × 2 (D0VX32) Cytochrome b-c1 complex subunit 6 × 2 (D0VX28) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein × 2 (D0VX27) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0VX26_CHICK
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 1–241 Author chain Q; PDBConstruct 1–241; UniProt 1–241

Cytochrome b-c1 complex subunit Rieske, mitochondrial

OrganismNot specified

UniProt Q5ZLR5

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 77–272 Chain I; UniProt 2–76 Chain R; UniProt 77–272 Chain V; UniProt 2–76 Fragment:UNP RESIDUES 77-272 Fragment:UNP RESIDUES 45-76 Non-standard monomer:Yes (specific site not provided by mmCIF) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i × 2 (D0VX31) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 × 2 (D0VX29) Cytochrome b × 2 (P18946) Mitochondrial cytochrome c1, heme protein × 2 (D0VX26) Cytochrome b-c1 complex subunit 7 × 2 (D0VX30) Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c × 2 (D0VX32) Cytochrome b-c1 complex subunit 6 × 2 (D0VX28) Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein × 2 (D0VX27) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRI_CHICK
Isoform
PDB entities 5, 9
Chains and sequence ranges Author chain E; PDBConstruct 1–196; UniProt 77–272 Author chain R; PDBConstruct 1–196; UniProt 77–272 Author chain I; PDBConstruct 2–76; UniProt 2–76 Author chain V; PDBConstruct 2–76; UniProt 2–76

Cytochrome b-c1 complex subunit 7

OrganismNot specified

UniProt D0VX30

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 1–110 Chain S; UniProt 1–110 Not recorded Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i × 2 (D0VX31) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 × 2 (D0VX29) Cytochrome b × 2 (P18946) Mitochondrial cytochrome c1, heme protein × 2 (D0VX26) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c × 2 (D0VX32) Cytochrome b-c1 complex subunit 6 × 2 (D0VX28) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein × 2 (D0VX27) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0VX30_CHICK
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–110; UniProt 1–110 Author chain S; PDBConstruct 1–110; UniProt 1–110

Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c

OrganismNot specified

UniProt D0VX32

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 1–81 Chain T; UniProt 1–81 Not recorded Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i × 2 (D0VX31) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 × 2 (D0VX29) Cytochrome b × 2 (P18946) Mitochondrial cytochrome c1, heme protein × 2 (D0VX26) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Cytochrome b-c1 complex subunit 7 × 2 (D0VX30) Cytochrome b-c1 complex subunit 6 × 2 (D0VX28) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein × 2 (D0VX27) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0VX32_CHICK
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–81; UniProt 1–81 Author chain T; PDBConstruct 1–81; UniProt 1–81

Cytochrome b-c1 complex subunit 6

OrganismNot specified

UniProt D0VX28

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 1–77 Chain U; UniProt 1–77 Not recorded Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i × 2 (D0VX31) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 × 2 (D0VX29) Cytochrome b × 2 (P18946) Mitochondrial cytochrome c1, heme protein × 2 (D0VX26) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Cytochrome b-c1 complex subunit 7 × 2 (D0VX30) Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c × 2 (D0VX32) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein × 2 (D0VX27) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0VX28_CHICK
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–77; UniProt 1–77 Author chain U; PDBConstruct 1–77; UniProt 1–77

Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein

OrganismNot specified

UniProt D0VX27

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 1–61 Chain W; UniProt 1–61 Not recorded Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i × 2 (D0VX31) Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 × 2 (D0VX29) Cytochrome b × 2 (P18946) Mitochondrial cytochrome c1, heme protein × 2 (D0VX26) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) Cytochrome b-c1 complex subunit 7 × 2 (D0VX30) Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c × 2 (D0VX32) Cytochrome b-c1 complex subunit 6 × 2 (D0VX28) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 2 (Q5ZLR5) PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 14 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 Y52 methyl (2E)-3-methoxy-2-(2-{[(5-methoxy-1,3-benzothiazol-2-yl)sulfanyl]methyl}phenyl)prop-2-enoate × 2 U10 UBIQUINONE-10 × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 GOL GLYCEROL × 2 HEC HEME C × 2 CDL CARDIOLIPIN × 4 BOG octyl beta-D-glucopyranoside × 3 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.77;278 K;CRYSTALLIZATION CONDITIONS: 50 MM CACODYLATE, 9.4 MM TRISHCL, 30 MM K-MES, 1.8 MM K-MOPS, 30 MM NACL, 31 MM KCL, 10 MM MGCL2, 91 G/L GLYCEROL, 30 G/L PEG 4KDA, 0.9 MM NAN3, 0.05 MM EDTA, 0.47G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, TEMPERATURE 278K Resolution 3.23 Å R-free 0.284

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0VX27_CHICK
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–61; UniProt 1–61 Author chain W; PDBConstruct 1–61; UniProt 1–61

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 4u3f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4u3f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4u3f
Deposition date deposition_date2014-07-21
Structure title titleCytochrome bc1 complex from chicken with designed inhibitor bound
Keywords keywords;CYTOCHROME BC1, MEMBRANE PROTEIN, HEME PROTEIN, RIESKE IRON SULFUR PROTEIN, CYTOCHROME B, CYTOCHROME C1, UBIQUINONE, COMPLEX III, STROBILURINS, AZOXYSTROBIN, STIGMATELLIN, OXIDOREDUCTASE, REDOX ENZYME RESPIRATORY CHAIN, ELECTRON TRANSPORT, HEME, INNER MEMBRANE, MEMBRANE BINDING, MITOCHONDRION, TRANSMEMBRANE, IRON, MITOCHONDRIAL INNER MEMBRANE, RESPIRATORY CHAIN, 2FE-2S, IRON-SULFUR, METAL-BINDING, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex ;; OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier55.33
Radius of gyration Rg (electron density) rg_electron54.33
Forward intensity I(0) i02947760000.00
Molecular weight molecular_weight465330.0 kDa
Excluded volume excluded_volume585780 ų
Envelope volume envelope_volume815920 ų
Hydration-shell volume shell_volume120770 ų
Envelope diameter envelope_diameter173.3
Shell Rg shell_rg59.96
Envelope Rg envelope_rg53.65
Shape Rg shape_rg54.32
Total Rg total_rg54.51
Total atoms total_atoms32759
Residues n_residues4063
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 dmax175.9
Rg (real space) rg_real55.20
Rg uncertainty (real space) rg_real_error1.40
I(0) (real space) i0_real2.9480e+09
I(0) uncertainty (real space) i0_real_error5.5980e+07
Rg (reciprocal space) rg_reciprocal55.41
I(0) (reciprocal space) i0_reciprocal2949000000.0000
Solution quality estimate total_estimate0.8678
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.8
Skewness Skewness skewness0.222
Kurtosis Kurtosis kurtosis-0.575
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha279900000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.987; Smooth: 0.484

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (21)

7. Fold Classification (SCOP + CATH) 28 domains

CATH v4.4 (28 domains)

Domain ID domain_id4u3fA01
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_id4u3fA02
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_id4u3fB01
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_id4u3fB02
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_id4u3fC00
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_id4u3fD01
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_id4u3fD02
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_id4u3fE01
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_id4u3fE02
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_id4u3fF00
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_id4u3fG00
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_id4u3fH00
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_id4u3fI00
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_id4u3fJ00
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_id4u3fN01
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_id4u3fN02
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_id4u3fO01
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_id4u3fO02
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_id4u3fP00
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_id4u3fQ01
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_id4u3fQ02
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_id4u3fR01
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_id4u3fR02
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_id4u3fS00
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_id4u3fT00
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_id4u3fU00
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_id4u3fV00
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_id4u3fW00
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

8. Citations (1)

9. Files and Curves (10)