9tao

Local refinement of E. coli Complex I D79N NuoA mutant membrane domain in LMNG

Method: ELECTRON MICROSCOPY
▼

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

NADH-quinone oxidoreductase subunit H

Escherichia coli BW25113

UniProt P0AFD4

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 7 NADH-quinone oxidoreductase subunit K × 1 (P0AFE4) NADH-quinone oxidoreductase subunit L × 1 (P33607) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit J × 1 (P0AFE0) NADH-quinone oxidoreductase subunit M × 1 (P0AFE8) NADH-quinone oxidoreductase subunit N × 1 (P0AFF0) 1,2-Distearoyl-sn-glycerophosphoethanolamine × 12 (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 5 CARDIOLIPIN × 1 Ubiquinone-8 × 2 water × 7 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOH_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain H; PDBConstruct 1–325; UniProt 1–325

NADH-quinone oxidoreductase subunit K

Escherichia coli BW25113

UniProt P0AFE4

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 7 NADH-quinone oxidoreductase subunit H × 1 (P0AFD4) NADH-quinone oxidoreductase subunit L × 1 (P33607) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit J × 1 (P0AFE0) NADH-quinone oxidoreductase subunit M × 1 (P0AFE8) NADH-quinone oxidoreductase subunit N × 1 (P0AFF0) 1,2-Distearoyl-sn-glycerophosphoethanolamine × 12 (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 5 CARDIOLIPIN × 1 Ubiquinone-8 × 2 water × 7 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOK_ECOLI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–100; UniProt 1–100

NADH-quinone oxidoreductase subunit L

Escherichia coli BW25113

UniProt P33607

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 7 NADH-quinone oxidoreductase subunit H × 1 (P0AFD4) NADH-quinone oxidoreductase subunit K × 1 (P0AFE4) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit J × 1 (P0AFE0) NADH-quinone oxidoreductase subunit M × 1 (P0AFE8) NADH-quinone oxidoreductase subunit N × 1 (P0AFF0) 1,2-Distearoyl-sn-glycerophosphoethanolamine × 12 (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 5 CARDIOLIPIN × 1 Ubiquinone-8 × 2 water × 7 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOL_ECOLI
Isoform —
PDB entities 3
Chains and sequence ranges Author chain L; PDBConstruct 1–613; UniProt 1–613

NADH-quinone oxidoreductase subunit A

Escherichia coli BW25113

UniProt P0AFC3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 7 NADH-quinone oxidoreductase subunit H × 1 (P0AFD4) NADH-quinone oxidoreductase subunit K × 1 (P0AFE4) NADH-quinone oxidoreductase subunit L × 1 (P33607) NADH-quinone oxidoreductase subunit J × 1 (P0AFE0) NADH-quinone oxidoreductase subunit M × 1 (P0AFE8) NADH-quinone oxidoreductase subunit N × 1 (P0AFF0) 1,2-Distearoyl-sn-glycerophosphoethanolamine × 12 (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 5 CARDIOLIPIN × 1 Ubiquinone-8 × 2 water × 7 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOA_ECOLI
Isoform —
PDB entities 4
Chains and sequence ranges Author chain A; PDBConstruct 1–147; UniProt 1–147

NADH-quinone oxidoreductase subunit J

Escherichia coli BW25113

UniProt P0AFE0

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 7 NADH-quinone oxidoreductase subunit H × 1 (P0AFD4) NADH-quinone oxidoreductase subunit K × 1 (P0AFE4) NADH-quinone oxidoreductase subunit L × 1 (P33607) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit M × 1 (P0AFE8) NADH-quinone oxidoreductase subunit N × 1 (P0AFF0) 1,2-Distearoyl-sn-glycerophosphoethanolamine × 12 (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 5 CARDIOLIPIN × 1 Ubiquinone-8 × 2 water × 7 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOJ_ECOLI
Isoform —
PDB entities 5
Chains and sequence ranges Author chain J; PDBConstruct 1–184; UniProt 1–184

NADH-quinone oxidoreductase subunit M

Escherichia coli BW25113

UniProt P0AFE8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 7 NADH-quinone oxidoreductase subunit H × 1 (P0AFD4) NADH-quinone oxidoreductase subunit K × 1 (P0AFE4) NADH-quinone oxidoreductase subunit L × 1 (P33607) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit J × 1 (P0AFE0) NADH-quinone oxidoreductase subunit N × 1 (P0AFF0) 1,2-Distearoyl-sn-glycerophosphoethanolamine × 12 (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 5 CARDIOLIPIN × 1 Ubiquinone-8 × 2 water × 7 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOM_ECOLI
Isoform —
PDB entities 6
Chains and sequence ranges Author chain M; PDBConstruct 1–509; UniProt 1–509

NADH-quinone oxidoreductase subunit N

Escherichia coli BW25113

UniProt P0AFF0

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 7 NADH-quinone oxidoreductase subunit H × 1 (P0AFD4) NADH-quinone oxidoreductase subunit K × 1 (P0AFE4) NADH-quinone oxidoreductase subunit L × 1 (P33607) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit J × 1 (P0AFE0) NADH-quinone oxidoreductase subunit M × 1 (P0AFE8) 1,2-Distearoyl-sn-glycerophosphoethanolamine × 12 (1R)-2-(dodecanoyloxy)-1-[(phosphonooxy)methyl]ethyl tetradecanoate × 5 CARDIOLIPIN × 1 Ubiquinone-8 × 2 water × 7 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUON_ECOLI
Isoform —
PDB entities 7
Chains and sequence ranges Author chain N; PDBConstruct 1–485; UniProt 1–485

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id9tao
Deposition date deposition_date2025-11-18
Structure title titleLocal refinement of E. coli Complex I D79N NuoA mutant membrane domain in LMNG
Keywords keywordsPROTON TRANSPORT, bioenergetics; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY
▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

9tao__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

9tao__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9tao__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)52.00 Å
Rg (electron density)52.48 Å
Total Rg52.38 Å
Atom count18587
Residues2281
Excluded volume346240 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9tao__assembly_1__model_1 heptameric (7) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (12)

▶

7. Citations (2)