4he8

Crystal structure of the membrane domain of respiratory complex I from Thermus thermophilus

Method: X-RAY DIFFRACTION Dmax: 205.0 Å Quality: GOOD

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

NADH-quinone oxidoreductase subunit 7

OrganismNot specified

UniProt Q56217

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–119 Not recorded NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain B; UniProt 1–119 Not recorded NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO7_THET8
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–119; UniProt 1–119 Author chain B; PDBConstruct 1–119; UniProt 1–119

NADH-quinone oxidoreductase subunit 10

OrganismNot specified

UniProt Q56225

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain J; UniProt 1–176 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 1–176 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO10_THET8
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–176; UniProt 1–176 Author chain J; PDBConstruct 1–176; UniProt 1–176

NADH-quinone oxidoreductase subunit 11

OrganismNot specified

UniProt Q56226

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain K; UniProt 1–95 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 1–95 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO11_THET8
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–95; UniProt 1–95 Author chain K; PDBConstruct 1–95; UniProt 1–95

NADH-quinone oxidoreductase subunit 12

OrganismNot specified

UniProt Q56227

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain L; UniProt 1–606 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain F; UniProt 1–606 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO12_THET8
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–606; UniProt 1–606 Author chain L; PDBConstruct 1–606; UniProt 1–606

NADH-quinone oxidoreductase subunit 13

OrganismNot specified

UniProt Q56228

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain M; UniProt 1–469 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain G; UniProt 1–469 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO13_THET8
Isoform
PDB entities 5
Chains and sequence ranges Author chain G; PDBConstruct 1–469; UniProt 1–469 Author chain M; PDBConstruct 1–469; UniProt 1–469

NADH-quinone oxidoreductase subunit 14

OrganismNot specified

UniProt Q56229

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain N; UniProt 1–427 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain I; UniProt 1–427 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO14_THET8
Isoform
PDB entities 6
Chains and sequence ranges Author chain I; PDBConstruct 1–427; UniProt 1–427 Author chain N; PDBConstruct 1–427; UniProt 1–427

NADH-quinone oxidoreductase subunit 8

OrganismNot specified

UniProt Q60019

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 1–365 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263
2 Protein heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–365 Not recorded NADH-quinone oxidoreductase subunit 7 × 1 (Q56217) NADH-quinone oxidoreductase subunit 10 × 1 (Q56225) NADH-quinone oxidoreductase subunit 11 × 1 (Q56226) NADH-quinone oxidoreductase subunit 12 × 1 (Q56227) NADH-quinone oxidoreductase subunit 13 × 1 (Q56228) NADH-quinone oxidoreductase subunit 14 × 1 (Q56229) UMQ UNDECYL-MALTOSIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.5;290 K;100 mM phosphate-citrate pH 4.5, 26% (v/v) PEG300, 5 mM CHAPS, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 3.30 Å R-free 0.263

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.

11 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO8_THET8
Isoform
PDB entities 7
Chains and sequence ranges Author chain C; PDBConstruct 1–365; UniProt 1–365 Author chain H; PDBConstruct 1–365; UniProt 1–365

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 4he8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4he8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4he8
Deposition date deposition_date2012-10-03
Structure title titleCrystal structure of the membrane domain of respiratory complex I from Thermus thermophilus
Keywords keywordsNADH-quinone oxidoreductase, complex I, oxidoreductase, proton pump, membrane protein, NADH, menaquinone, cytoplasmic membrane; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.48
Radius of gyration Rg (electron density) rg_electron61.04
Forward intensity I(0) i02155360000.00
Molecular weight molecular_weight459890.0 kDa
Excluded volume excluded_volume603120 ų
Envelope volume envelope_volume773780 ų
Hydration-shell volume shell_volume108810 ų
Envelope diameter envelope_diameter229.6
Shell Rg shell_rg58.77
Envelope Rg envelope_rg61.01
Shape Rg shape_rg61.08
Total Rg total_rg60.82
Total atoms total_atoms32650
Residues n_residues4286
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 dmax205.0
Rg (real space) rg_real61.00
Rg uncertainty (real space) rg_real_error2.19
I(0) (real space) i0_real2.1550e+09
I(0) uncertainty (real space) i0_real_error4.7460e+07
Rg (reciprocal space) rg_reciprocal60.02
I(0) (reciprocal space) i0_reciprocal2152000000.0000
Solution quality estimate total_estimate0.8409
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.0
Skewness Skewness skewness0.573
Kurtosis Kurtosis kurtosis-0.045
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha199600000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.441

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 15 domains

SCOP 2.08 (7 domains)

Domain ID domain_idd4he8a_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.73 — Non-antiporter membrane subunits from respiratory complex I
Superfamily Superfamily superfamilyf.73.3 — Respiratory complex I subunit NuoA-like
Family Family familyf.73.3.1 — Respiratory complex I subunit NuoA-like
Domain ID domain_idd4he8c_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.72 — Antiporter-like subunits from respiratory complex I
Superfamily Superfamily superfamilyf.72.1 — Antiporter-like subunits from respiratory complex I
Family Family familyf.72.1.2 — Single antiporter-like subunits from respiratory complex I
Domain ID domain_idd4he8j_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.73 — Non-antiporter membrane subunits from respiratory complex I
Superfamily Superfamily superfamilyf.73.2 — Respiratory complex I subunit NuoJ-like
Family Family familyf.73.2.1 — Respiratory complex I subunit NuoJ-like
Domain ID domain_idd4he8k_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.73 — Non-antiporter membrane subunits from respiratory complex I
Superfamily Superfamily superfamilyf.73.1 — Respiratory complex I subunit NuoK-like
Family Family familyf.73.1.1 — Respiratory complex I subunit NuoK-like
Domain ID domain_idd4he8l_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.72 — Antiporter-like subunits from respiratory complex I
Superfamily Superfamily superfamilyf.72.1 — Antiporter-like subunits from respiratory complex I
Family Family familyf.72.1.1 — Double antiporter-like subunits from respiratory complex I
Domain ID domain_idd4he8m_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.72 — Antiporter-like subunits from respiratory complex I
Superfamily Superfamily superfamilyf.72.1 — Antiporter-like subunits from respiratory complex I
Family Family familyf.72.1.1 — Double antiporter-like subunits from respiratory complex I
Domain ID domain_idd4he8n_
Class classf — Membrane and cell surface proteins and peptides
Fold Fold foldf.72 — Antiporter-like subunits from respiratory complex I
Superfamily Superfamily superfamilyf.72.1 — Antiporter-like subunits from respiratory complex I
Family Family familyf.72.1.1 — Double antiporter-like subunits from respiratory complex I

CATH v4.4 (8 domains)

Domain ID domain_id4he8A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily1610 — NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
Domain ID domain_id4he8B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily1610 — NADH:ubiquinone/plastoquinone oxidoreductase, chain 3
Domain ID domain_id4he8D00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1200 — NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ
Domain ID domain_id4he8E00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3510
Domain ID domain_id4he8F02
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 superfamily2700
Domain ID domain_id4he8J00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily1200 — NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ
Domain ID domain_id4he8K00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3510
Domain ID domain_id4he8L02
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 superfamily2700

8. Citations (1)

9. Files and Curves (10)