3bcc

STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN

Method: X-RAY DIFFRACTION

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

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

UniProt P31800

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: 20-MERIC(20) Consistent with protein copy count Chain A; UniProt 35–480 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P23004) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P18946) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00125) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13272) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00129) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13271) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00126) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

46 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCR1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–446; UniProt 35–480

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

UniProt P23004

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: 20-MERIC(20) Consistent with protein copy count Chain B; UniProt 32–453 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P31800) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P18946) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00125) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13272) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00129) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13271) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00126) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCR2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–422; UniProt 32–453

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

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: 20-MERIC(20) Consistent with protein copy count Chain C; UniProt 1–380 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P31800) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P23004) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00125) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13272) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00129) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13271) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00126) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

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 1–380; UniProt 1–380

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

UniProt P00125

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: 20-MERIC(20) Consistent with protein copy count Chain D; UniProt 1–241 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P31800) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P23004) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P18946) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13272) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00129) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13271) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00126) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CY1_BOVIN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 1–241

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

UniProt P13272

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: 20-MERIC(20) Consistent with protein copy count Chain E; UniProt 79–274 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P31800) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P23004) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P18946) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00125) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00129) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13271) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00126) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

48 other PDB entries and 53 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRI_BOVIN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–196; UniProt 79–274

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

UniProt P00129

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: 20-MERIC(20) Consistent with protein copy count Chain F; UniProt 1–109 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P31800) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P23004) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P18946) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00125) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13272) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13271) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00126) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

45 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCR6_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–109; UniProt 1–109

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

UniProt P13271

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: 20-MERIC(20) Consistent with protein copy count Chain G; UniProt 1–81 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P31800) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P23004) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P18946) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00125) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13272) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00129) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00126) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

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

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

UniProt P00126

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: 20-MERIC(20) Consistent with protein copy count Chain H; UniProt 1–78 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P31800) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P23004) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P18946) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00125) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13272) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00129) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13271) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00130) HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

46 other PDB entries and 51 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRH_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–78; UniProt 1–78

UBIQUINOL CYTOCHROME C OXIDOREDUCTASE

OrganismNot specified

UniProt P00130

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 20 PDB declaration: 20-MERIC(20) Consistent with protein copy count Chain J; UniProt 1–62 Not recorded UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P31800) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P23004) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P18946) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00125) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13272) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00129) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P13271) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 (P00126) UBIQUINOL CYTOCHROME C OXIDOREDUCTASE × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 6 SIG STIGMATELLIN × 2 AMY ANTIMYCIN × 2 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.7;20MM KMES PH6.7, 75MM NACL, 10% GLYCEROL, AND 6% PEG4000, INHIBITOR WAS ADDED FROM ETHANOLIC SOLUTION Resolution 3.70 Å R-free 0.321

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

47 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UCRX_BOVIN
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–62; UniProt 1–62

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

暂无 SAXS 图

P(r) Distance Distribution P(r) Distribution

暂无 P(r) 图
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3bcc
Deposition date deposition_date1998-03-23
Structure title titleSTIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN
Keywords keywordsUBIQUINONE, OXIDOREDUCTASE, REDOX ENZYME, MEMBRANE PROTEIN, RESPIRATORY CHAIN, STIGMATELLIN, ANTIMYCIN, ELECTRON TRANSPORT; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

该条目暂无 SAXS 数据。

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

该条目暂无 P(r) 分析数据。

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 27 domains

SCOP 2.08 (14 domains)

Domain ID domain_idd3bcca1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.1 — MPP-like
Domain ID domain_idd3bcca2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.1 — MPP-like
Domain ID domain_idd3bccb1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.1 — MPP-like
Domain ID domain_idd3bccb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.185 — LuxS/MPP-like metallohydrolase
Superfamily Superfamily superfamilyd.185.1 — LuxS/MPP-like metallohydrolase
Family Family familyd.185.1.1 — MPP-like
Domain ID domain_idd3bccc2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.32 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.32.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.32.1.1 — a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3bccc3
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.21 — Heme-binding four-helical bundle
Superfamily Superfamily superfamilyf.21.1 — Transmembrane di-heme cytochromes
Family Family familyf.21.1.2 — Cytochrome b of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3bccd2
Class classa — All alpha proteins
Fold Fold folda.3 — Cytochrome c
Superfamily Superfamily superfamilya.3.1 — Cytochrome c
Family Family familya.3.1.3 — Cytochrome bc1 domain
Domain ID domain_idd3bccd3
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.11 — Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor
Family Family familyf.23.11.1 — Cytochrome c1 subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase), transmembrane anchor
Domain ID domain_idd3bcce1
Class classb — All beta proteins
Fold Fold foldb.33 — ISP domain
Superfamily Superfamily superfamilyb.33.1 — ISP domain
Family Family familyb.33.1.1 — Rieske iron-sulfur protein (ISP)
Domain ID domain_idd3bcce2
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.12 — ISP transmembrane anchor
Family Family familyf.23.12.1 — ISP transmembrane anchor
Domain ID domain_idd3bccf_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.27 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.27.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.27.1.1 — 14 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3bccg_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.13 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.23.13.1 — Ubiquinone-binding protein QP-C of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3bcch_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.28 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Superfamily Superfamily superfamilyf.28.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.28.1.1 — Non-heme 11 kDa protein of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Domain ID domain_idd3bccj_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.23 — Single transmembrane helix
Superfamily Superfamily superfamilyf.23.14 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)
Family Family familyf.23.14.1 — Subunit X (non-heme 7 kDa protein) of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)

CATH v4.4 (13 domains)

Domain ID domain_id3bccA01
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_id3bccA02
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_id3bccB01
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_id3bccB02
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_id3bccC00
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_id3bccD01
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_id3bccD02
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_id3bccE01
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_id3bccE02
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_id3bccF00
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_id3bccG00
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_id3bccH00
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_id3bccJ00
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 (0)