9tal

Local refinement of E. coli Complex I WT hydrophilic domain in LMNG

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

NADH-quinone oxidoreductase subunit E

Escherichia coli BW25113

UniProt P0AFD1

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 NADH-quinone oxidoreductase subunit F × 1 (P31979) NADH-quinone oxidoreductase subunit G × 1 (P33602) NADH-quinone oxidoreductase subunit I × 1 (P0AFD6) NADH-quinone oxidoreductase subunit B × 1 (P0AFC7) NADH-quinone oxidoreductase subunit C/D × 1 (P33599) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit H × 4 (P0AFD4) FE2/S2 (INORGANIC) CLUSTER × 2 CALCIUM ION × 5 FLAVIN MONONUCLEOTIDE × 1 IRON/SULFUR CLUSTER × 7 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOE_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–166; UniProt 1–166

NADH-quinone oxidoreductase subunit F

Escherichia coli BW25113

UniProt P31979

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 NADH-quinone oxidoreductase subunit E × 1 (P0AFD1) NADH-quinone oxidoreductase subunit G × 1 (P33602) NADH-quinone oxidoreductase subunit I × 1 (P0AFD6) NADH-quinone oxidoreductase subunit B × 1 (P0AFC7) NADH-quinone oxidoreductase subunit C/D × 1 (P33599) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit H × 4 (P0AFD4) FE2/S2 (INORGANIC) CLUSTER × 2 CALCIUM ION × 5 FLAVIN MONONUCLEOTIDE × 1 IRON/SULFUR CLUSTER × 7 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOF_ECOLI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain F; PDBConstruct 18–461; UniProt 2–445

NADH-quinone oxidoreductase subunit G

Escherichia coli BW25113

UniProt P33602

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 NADH-quinone oxidoreductase subunit E × 1 (P0AFD1) NADH-quinone oxidoreductase subunit F × 1 (P31979) NADH-quinone oxidoreductase subunit I × 1 (P0AFD6) NADH-quinone oxidoreductase subunit B × 1 (P0AFC7) NADH-quinone oxidoreductase subunit C/D × 1 (P33599) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit H × 4 (P0AFD4) FE2/S2 (INORGANIC) CLUSTER × 2 CALCIUM ION × 5 FLAVIN MONONUCLEOTIDE × 1 IRON/SULFUR CLUSTER × 7 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOG_ECOLI
Isoform —
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 3–910; UniProt 1–908

NADH-quinone oxidoreductase subunit I

Escherichia coli BW25113

UniProt P0AFD6

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 NADH-quinone oxidoreductase subunit E × 1 (P0AFD1) NADH-quinone oxidoreductase subunit F × 1 (P31979) NADH-quinone oxidoreductase subunit G × 1 (P33602) NADH-quinone oxidoreductase subunit B × 1 (P0AFC7) NADH-quinone oxidoreductase subunit C/D × 1 (P33599) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit H × 4 (P0AFD4) FE2/S2 (INORGANIC) CLUSTER × 2 CALCIUM ION × 5 FLAVIN MONONUCLEOTIDE × 1 IRON/SULFUR CLUSTER × 7 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOI_ECOLI
Isoform —
PDB entities 4
Chains and sequence ranges Author chain I; PDBConstruct 1–180; UniProt 1–180

NADH-quinone oxidoreductase subunit B

Escherichia coli BW25113

UniProt P0AFC7

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 NADH-quinone oxidoreductase subunit E × 1 (P0AFD1) NADH-quinone oxidoreductase subunit F × 1 (P31979) NADH-quinone oxidoreductase subunit G × 1 (P33602) NADH-quinone oxidoreductase subunit I × 1 (P0AFD6) NADH-quinone oxidoreductase subunit C/D × 1 (P33599) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit H × 4 (P0AFD4) FE2/S2 (INORGANIC) CLUSTER × 2 CALCIUM ION × 5 FLAVIN MONONUCLEOTIDE × 1 IRON/SULFUR CLUSTER × 7 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOB_ECOLI
Isoform —
PDB entities 5
Chains and sequence ranges Author chain B; PDBConstruct 1–220; UniProt 1–220

NADH-quinone oxidoreductase subunit C/D

Escherichia coli BW25113

UniProt P33599

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 11 NADH-quinone oxidoreductase subunit E × 1 (P0AFD1) NADH-quinone oxidoreductase subunit F × 1 (P31979) NADH-quinone oxidoreductase subunit G × 1 (P33602) NADH-quinone oxidoreductase subunit I × 1 (P0AFD6) NADH-quinone oxidoreductase subunit B × 1 (P0AFC7) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) NADH-quinone oxidoreductase subunit H × 4 (P0AFD4) FE2/S2 (INORGANIC) CLUSTER × 2 CALCIUM ION × 5 FLAVIN MONONUCLEOTIDE × 1 IRON/SULFUR CLUSTER × 7 water × 6 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NUOCD_ECOLI
Isoform —
PDB entities 6
Chains and sequence ranges Author chain C; PDBConstruct 5–600; UniProt 1–596

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 11 NADH-quinone oxidoreductase subunit E × 1 (P0AFD1) NADH-quinone oxidoreductase subunit F × 1 (P31979) NADH-quinone oxidoreductase subunit G × 1 (P33602) NADH-quinone oxidoreductase subunit I × 1 (P0AFD6) NADH-quinone oxidoreductase subunit B × 1 (P0AFC7) NADH-quinone oxidoreductase subunit C/D × 1 (P33599) NADH-quinone oxidoreductase subunit H × 4 (P0AFD4) FE2/S2 (INORGANIC) CLUSTER × 2 CALCIUM ION × 5 FLAVIN MONONUCLEOTIDE × 1 IRON/SULFUR CLUSTER × 7 water × 6 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 7
Chains and sequence ranges Author chain A; PDBConstruct 1–147; UniProt 1–147

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 11 NADH-quinone oxidoreductase subunit E × 1 (P0AFD1) NADH-quinone oxidoreductase subunit F × 1 (P31979) NADH-quinone oxidoreductase subunit G × 1 (P33602) NADH-quinone oxidoreductase subunit I × 1 (P0AFD6) NADH-quinone oxidoreductase subunit B × 1 (P0AFC7) NADH-quinone oxidoreductase subunit C/D × 1 (P33599) NADH-quinone oxidoreductase subunit A × 1 (P0AFC3) FE2/S2 (INORGANIC) CLUSTER × 2 CALCIUM ION × 5 FLAVIN MONONUCLEOTIDE × 1 IRON/SULFUR CLUSTER × 7 water × 6 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 8
Chains and sequence ranges Author chain H; PDBConstruct 1–325; UniProt 1–325 Author chain J; PDBConstruct 1–325; UniProt 1–325 Author chain K; PDBConstruct 1–325; UniProt 1–325 Author chain L; PDBConstruct 1–325; UniProt 1–325

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id9tal
Deposition date deposition_date2025-11-18
Structure title titleLocal refinement of E. coli Complex I WT hydrophilic domain in LMNG
Keywords keywordsPROTON TRANSPORT, bioenergetics; PROTON TRANSPORT
Experimental Method methodELECTRON MICROSCOPY
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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.

9tal__assembly_1__model_1

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

Download this curve (.dat)

9tal__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

9tal__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)44.67 Å
Rg (electron density)45.09 Å
Total Rg45.02 Å
Atom count20167
Residues2552
Excluded volume358660 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9tal__assembly_1__model_1 11-meric (11) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (13)

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7. Citations (1)