5nmi

Cytochrome bc1 bound to the inhibitor MJM170

Method: X-RAY DIFFRACTION Dmax: 177.0 Å Quality: GOOD

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

Cytochrome b-c1 complex subunit 1, mitochondrial

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain A; UniProt 36–479 Chain N; UniProt 36–479 Not recorded Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 4 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P00130) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 QCR1_BOVIN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–444; UniProt 36–479 Author chain N; PDBConstruct 1–444; UniProt 36–479

Cytochrome b-c1 complex subunit 2, mitochondrial

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain B; UniProt 31–453 Chain O; UniProt 31–453 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 4 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P00130) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 QCR2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–423; UniProt 31–453 Author chain O; PDBConstruct 1–423; UniProt 31–453

Cytochrome b

OrganismNot specified

UniProt P00157

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 C; UniProt 8–379 Chain P; UniProt 8–379 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 4 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P00130) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 CYB_BOVIN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–372; UniProt 8–379 Author chain P; PDBConstruct 1–372; UniProt 8–379

Cytochrome c1, heme protein, mitochondrial

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain D; UniProt 86–325 Chain Q; UniProt 86–325 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 4 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P00130) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 1–240; UniProt 86–325 Author chain Q; PDBConstruct 1–240; UniProt 86–325

Cytochrome b-c1 complex subunit Rieske, mitochondrial

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain E; UniProt 1–274 Chain I; UniProt 1–274 Chain R; UniProt 1–274 Chain V; UniProt 1–274 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P00130) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 1–274; UniProt 1–274 Author chain I; PDBConstruct 1–274; UniProt 1–274 Author chain R; PDBConstruct 1–274; UniProt 1–274 Author chain V; PDBConstruct 1–274; UniProt 1–274

Cytochrome b-c1 complex subunit 7

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain F; UniProt 1–111 Chain S; UniProt 1–111 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 4 (P13272) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P00130) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 QCR7_BOVIN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–111; UniProt 1–111 Author chain S; PDBConstruct 1–111; UniProt 1–111

Cytochrome b-c1 complex subunit 8

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain G; UniProt 1–82 Chain T; UniProt 1–82 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 4 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) Cytochrome b-c1 complex subunit 9 × 2 (P00130) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 QCR8_BOVIN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–82; UniProt 1–82 Author chain T; PDBConstruct 1–82; UniProt 1–82

Cytochrome b-c1 complex subunit 6, mitochondrial

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain H; UniProt 1–91 Chain U; UniProt 1–91 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 4 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 9 × 2 (P00130) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 QCR6_BOVIN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–91; UniProt 1–91 Author chain U; PDBConstruct 1–91; UniProt 1–91

Cytochrome b-c1 complex subunit 9

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 × 22 PDB declaration: 22-meric(22) Consistent with protein copy count Chain J; UniProt 1–64 Chain W; UniProt 1–64 Not recorded Cytochrome b-c1 complex subunit 1, mitochondrial × 2 (P31800) Cytochrome b-c1 complex subunit 2, mitochondrial × 2 (P23004) Cytochrome b × 2 (P00157) Cytochrome c1, heme protein, mitochondrial × 2 (P00125) Cytochrome b-c1 complex subunit Rieske, mitochondrial × 4 (P13272) Cytochrome b-c1 complex subunit 7 × 2 (P00129) Cytochrome b-c1 complex subunit 8 × 2 (P13271) Cytochrome b-c1 complex subunit 6, mitochondrial × 2 (P00126) ARG-ASN-TRP-VAL-PRO-THR-ALA-GLN-LEU-TRP-GLY-ALA-VAL-GLY-ALA-VAL-GLY-LEU-VAL-SER-ALA-THR × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 MJM (4aS)-2-methyl-3-(4-phenoxyphenyl)-5,6,7,8-tetrahydroquinolin-4(4aH)-one × 2 PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 6 CDL CARDIOLIPIN × 6 HEC HEME C × 2 FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.8;277 K;10 % PEG4000, HECAMEG Resolution 3.50 Å R-free 0.268

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 QCR9_BOVIN
Isoform
PDB entities 9
Chains and sequence ranges Author chain J; PDBConstruct 1–64; UniProt 1–64 Author chain W; PDBConstruct 1–64; UniProt 1–64

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 5nmi

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id5nmi
Deposition date deposition_date2017-04-05
Structure title titleCytochrome bc1 bound to the inhibitor MJM170
Keywords keywordsmembrane protein, inhibitor complex; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier54.46
Radius of gyration Rg (electron density) rg_electron53.58
Forward intensity I(0) i02780830000.00
Molecular weight molecular_weight449520.0 kDa
Excluded volume excluded_volume565200 ų
Envelope volume envelope_volume795570 ų
Hydration-shell volume shell_volume120080 ų
Envelope diameter envelope_diameter173.0
Shell Rg shell_rg59.15
Envelope Rg envelope_rg52.70
Shape Rg shape_rg53.59
Total Rg total_rg53.72
Total atoms total_atoms31648
Residues n_residues3934
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax177.0
Rg (real space) rg_real54.34
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real2.7810e+09
I(0) uncertainty (real space) i0_real_error5.6930e+07
Rg (reciprocal space) rg_reciprocal54.55
I(0) (reciprocal space) i0_reciprocal2782000000.0000
Solution quality estimate total_estimate0.8831
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.1
Skewness Skewness skewness0.230
Kurtosis Kurtosis kurtosis-0.537
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha253600000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.908; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.767

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

7. Fold Classification (SCOP + CATH) 25 domains

CATH v4.4 (25 domains)

Domain ID domain_id5nmiA01
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_id5nmiA02
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_id5nmiB01
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_id5nmiB02
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_id5nmiC00
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_id5nmiD01
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_id5nmiD02
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_id5nmiE01
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_id5nmiE02
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_id5nmiF00
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_id5nmiG00
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_id5nmiH00
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_id5nmiJ00
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_id5nmiN01
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_id5nmiN02
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_id5nmiO01
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_id5nmiO02
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_id5nmiP00
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_id5nmiQ01
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_id5nmiQ02
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_id5nmiR00
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_id5nmiS00
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_id5nmiT00
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_id5nmiU00
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_id5nmiW00
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)