4hea

Crystal structure of the entire respiratory complex I from Thermus thermophilus

Method: X-RAY DIFFRACTION Dmax: 266.8 Å Quality: EXCELLENT

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

NADH-quinone oxidoreductase subunit 1

OrganismNot specified

UniProt Q56222

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 1; UniProt 1–438 Not recorded NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain B; UniProt 1–438 Not recorded NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO1_THET8
Isoform
PDB entities 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–438; UniProt 1–438 Author chain B; PDBConstruct 1–438; UniProt 1–438

NADH-quinone oxidoreductase subunit 2

OrganismNot specified

UniProt Q56221

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 2; UniProt 1–181 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain C; UniProt 1–181 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO2_THET8
Isoform
PDB entities 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–181; UniProt 1–181 Author chain C; PDBConstruct 1–181; UniProt 1–181

NADH-quinone oxidoreductase subunit 3

OrganismNot specified

UniProt Q56223

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 3; UniProt 1–783 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain D; UniProt 1–783 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO3_THET8
Isoform
PDB entities 3
Chains and sequence ranges Author chain 3; PDBConstruct 1–783; UniProt 1–783 Author chain D; PDBConstruct 1–783; UniProt 1–783

NADH-quinone oxidoreductase subunit 4

OrganismNot specified

UniProt Q56220

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 4; UniProt 1–409 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain E; UniProt 1–409 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO4_THET8
Isoform
PDB entities 4
Chains and sequence ranges Author chain 4; PDBConstruct 1–409; UniProt 1–409 Author chain E; PDBConstruct 1–409; UniProt 1–409

NADH-quinone oxidoreductase subunit 5

OrganismNot specified

UniProt Q56219

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 5; UniProt 1–207 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain F; UniProt 1–207 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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.

18 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO5_THET8
Isoform
PDB entities 5
Chains and sequence ranges Author chain 5; PDBConstruct 1–207; UniProt 1–207 Author chain F; PDBConstruct 1–207; UniProt 1–207

NADH-quinone oxidoreductase subunit 6

OrganismNot specified

UniProt Q56218

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 6; UniProt 1–181 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain G; UniProt 1–181 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO6_THET8
Isoform
PDB entities 6
Chains and sequence ranges Author chain 6; PDBConstruct 1–181; UniProt 1–181 Author chain G; PDBConstruct 1–181; UniProt 1–181

NADH-quinone oxidoreductase subunit 9

OrganismNot specified

UniProt Q56224

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 9; UniProt 1–182 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain O; UniProt 1–182 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO9_THET8
Isoform
PDB entities 7
Chains and sequence ranges Author chain 9; PDBConstruct 1–182; UniProt 1–182 Author chain O; PDBConstruct 1–182; UniProt 1–182

NADH-quinone oxidoreductase subunit 15

OrganismNot specified

UniProt Q5SKZ7

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain 7; UniProt 1–129 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain I; UniProt 1–129 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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.

15 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NQO15_THET8
Isoform
PDB entities 8
Chains and sequence ranges Author chain 7; PDBConstruct 1–129; UniProt 1–129 Author chain I; PDBConstruct 1–129; UniProt 1–129

Putative uncharacterized protein TTHA1528

OrganismNot specified

UniProt Q5SI52

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain W; UniProt 1–131 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain X; UniProt 1–131 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) 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) NADH-quinone oxidoreductase subunit 8 × 1 (Q60019) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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.

8 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q5SI52_THET8
Isoform
PDB entities 9
Chains and sequence ranges Author chain W; PDBConstruct 1–131; UniProt 1–131 Author chain X; PDBConstruct 1–131; UniProt 1–131

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 1–119 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain P; UniProt 1–119 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 10
Chains and sequence ranges Author chain A; PDBConstruct 1–119; UniProt 1–119 Author chain P; 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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain J; UniProt 1–176 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain R; UniProt 1–176 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 11
Chains and sequence ranges Author chain J; PDBConstruct 1–176; UniProt 1–176 Author chain R; 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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain K; UniProt 1–95 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain S; UniProt 1–95 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 12
Chains and sequence ranges Author chain K; PDBConstruct 1–95; UniProt 1–95 Author chain S; 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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain L; UniProt 1–606 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain T; UniProt 1–606 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 13
Chains and sequence ranges Author chain L; PDBConstruct 1–606; UniProt 1–606 Author chain T; 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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain M; UniProt 1–469 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain U; UniProt 1–469 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 14
Chains and sequence ranges Author chain M; PDBConstruct 1–469; UniProt 1–469 Author chain U; 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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain N; UniProt 1–427 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain V; UniProt 1–427 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 15
Chains and sequence ranges Author chain N; PDBConstruct 1–427; UniProt 1–427 Author chain V; 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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain H; UniProt 1–365 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239
2 Protein heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain Q; UniProt 1–365 Not recorded NADH-quinone oxidoreductase subunit 1 × 1 (Q56222) NADH-quinone oxidoreductase subunit 2 × 1 (Q56221) NADH-quinone oxidoreductase subunit 3 × 1 (Q56223) NADH-quinone oxidoreductase subunit 4 × 1 (Q56220) NADH-quinone oxidoreductase subunit 5 × 1 (Q56219) NADH-quinone oxidoreductase subunit 6 × 1 (Q56218) NADH-quinone oxidoreductase subunit 9 × 1 (Q56224) NADH-quinone oxidoreductase subunit 15 × 1 (Q5SKZ7) Putative uncharacterized protein TTHA1528 × 1 (Q5SI52) 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) SF4 IRON/SULFUR CLUSTER × 7 FMN FLAVIN MONONUCLEOTIDE × 1 FES FE2/S2 (INORGANIC) CLUSTER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 19% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 2.2 mM FOS-CHOLINE-8 fluorinated , VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 24% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 50 mM NDSB-201, VAPOR DIFFUSION, SITTING DROP, temperature 295K X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;295 K;100 mM Bis-Tris pH 6.0, 26% (w/v) polyethylene glycol (PEG) 4000, 100 mM KCl, 100 mM glutaric acid pH 6.0 and 0.6% DDM, VAPOR DIFFUSION, SITTING DROP, temperature 295K Resolution 3.30 Å R-free 0.239

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 16
Chains and sequence ranges Author chain H; PDBConstruct 1–365; UniProt 1–365 Author chain Q; 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 4hea

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4hea
Deposition date deposition_date2012-10-03
Structure title titleCrystal structure of the entire 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_guinier96.18
Radius of gyration Rg (electron density) rg_electron100.80
Forward intensity I(0) i013182700000.00
Molecular weight molecular_weight1050400.0 kDa
Excluded volume excluded_volume1342700 ų
Envelope volume envelope_volume2134300 ų
Hydration-shell volume shell_volume195120 ų
Envelope diameter envelope_diameter367.5
Shell Rg shell_rg77.03
Envelope Rg envelope_rg100.30
Shape Rg shape_rg101.00
Total Rg total_rg99.76
Total atoms total_atoms73998
Residues n_residues9540
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 dmax266.8
Rg (real space) rg_real90.13
Rg uncertainty (real space) rg_real_error1.37
I(0) (real space) i0_real1.2640e+10
I(0) uncertainty (real space) i0_real_error2.8250e+08
Rg (reciprocal space) rg_reciprocal90.47
I(0) (reciprocal space) i0_reciprocal12940000000.0000
Solution quality estimate total_estimate0.9164
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary116.7
Skewness Skewness skewness0.297
Kurtosis Kurtosis kurtosis-0.582
Angular range angular_range— – 0.0800 −1
Current regularization parameter α current_alpha0.5650
Highest regularization parameter α highest_alpha160200000.0000
Real-space data points n_real_points17
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.017; Oscil: 0.996; Stabil: 0.976; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (19)

7. Fold Classification (SCOP + CATH) 30 domains

CATH v4.4 (30 domains)

Domain ID domain_id4hea101
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1450
Domain ID domain_id4hea102
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11540 — NADH-ubiquinone oxidoreductase 51kDa subunit
Domain ID domain_id4hea103
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily600
Domain ID domain_id4hea104
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily230 — NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain
Domain ID domain_id4hea201
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily1590 — NADH-quinone oxidoreductase subunit E
Domain ID domain_id4hea202
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id4hea400
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology645 — Cytochrome-c3 Hydrogenase; chain B
Homologous superfamily homologous superfamily10 — Cytochrome-c3 Hydrogenase, chain B
Domain ID domain_id4hea600
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12280
Domain ID domain_id4hea700
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology920 — Metal Transport, Frataxin; Chain A
Homologous superfamily homologous superfamily80 — NADH-quinone oxidoreductase, subunit 15
Domain ID domain_id4hea900
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily3270
Domain ID domain_id4heaA00
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_id4heaB01
Class class6 — Special
Architecture architecture10 — Helix non-globular
Topology topology250 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily1450
Domain ID domain_id4heaB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11540 — NADH-ubiquinone oxidoreductase 51kDa subunit
Domain ID domain_id4heaB03
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily600
Domain ID domain_id4heaB04
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1440 — de novo design (two linked rop proteins)
Homologous superfamily homologous superfamily230 — NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain
Domain ID domain_id4heaC01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology10 — Arc Repressor Mutant, subunit A
Homologous superfamily homologous superfamily1590 — NADH-quinone oxidoreductase subunit E
Domain ID domain_id4heaC02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id4heaE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology645 — Cytochrome-c3 Hydrogenase; chain B
Homologous superfamily homologous superfamily10 — Cytochrome-c3 Hydrogenase, chain B
Domain ID domain_id4heaG00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily12280
Domain ID domain_id4heaI00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology920 — Metal Transport, Frataxin; Chain A
Homologous superfamily homologous superfamily80 — NADH-quinone oxidoreductase, subunit 15
Domain ID domain_id4heaJ00
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_id4heaK00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3510
Domain ID domain_id4heaL02
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_id4heaO00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily3270
Domain ID domain_id4heaP00
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_id4heaR00
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_id4heaS00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily3510
Domain ID domain_id4heaT02
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_id4heaW00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1530 — hypothetical protein tt1805
Homologous superfamily homologous superfamily10 — TTHA1528-like
Domain ID domain_id4heaX00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology1530 — hypothetical protein tt1805
Homologous superfamily homologous superfamily10 — TTHA1528-like

8. Citations (1)

9. Files and Curves (10)