9uv7

Single-subunit apo Escherichia coli nicotinamide nucleotide transhydrogenase

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

NAD(P) transhydrogenase subunit beta

Escherichia coli K-12

UniProt P0AB67

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 NAD(P) transhydrogenase subunit alpha × 2 (P07001) NAD(P) transhydrogenase subunit alpha × 2 (P07001) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PNTB_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–462; UniProt 1–462 Author chain B; PDBConstruct 1–462; UniProt 1–462

NAD(P) transhydrogenase subunit alpha

Escherichia coli K-12

UniProt P07001

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 6 NAD(P) transhydrogenase subunit beta × 2 (P0AB67) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PNTA_ECOLI
Isoform —
PDB entities 2, 3
Chains and sequence ranges Author chain C; PDBConstruct 1–97; UniProt 411–507 Author chain D; PDBConstruct 1–97; UniProt 411–507 Author chain E; PDBConstruct 4–377; UniProt 2–375 Author chain F; PDBConstruct 4–377; UniProt 2–375

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_id9uv7
Deposition date deposition_date2025-05-09
Structure title titleSingle-subunit apo Escherichia coli nicotinamide nucleotide transhydrogenase
Keywords keywords;Nicotinamide nucleotide transhydrogenase, Mitochondrial inner membrane, E. coli transhydrogenase, Hydride transfer, Proton motive force, NAD+, NADH, NADP+, NADPH, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
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.

9uv7__assembly_1__model_1

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

Download this curve (.dat)

9uv7__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.

9uv7__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)42.01 Å
Rg (electron density)41.96 Å
Total Rg42.25 Å
Atom count13484
Residues1802
Excluded volume244380 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9uv7__assembly_1__model_1 hexameric (6) 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 (3)

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7. Citations (1)