8orb

24-meric catalytic domain of dihydrolipoamide acetyltransferase (E2) of the E. coli pyruvate dehydrogenase complex.

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

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Escherichia coli

UniProt P06959

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 24 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ODP2_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–249; UniProt 382–630 Author chain B; PDBConstruct 1–249; UniProt 382–630 Author chain C; PDBConstruct 1–249; UniProt 382–630 Author chain D; PDBConstruct 1–249; UniProt 382–630 Author chain E; PDBConstruct 1–249; UniProt 382–630 Author chain F; PDBConstruct 1–249; UniProt 382–630 Author chain G; PDBConstruct 1–249; UniProt 382–630 Author chain H; PDBConstruct 1–249; UniProt 382–630 Author chain I; PDBConstruct 1–249; UniProt 382–630 Author chain J; PDBConstruct 1–249; UniProt 382–630 Author chain K; PDBConstruct 1–249; UniProt 382–630 Author chain L; PDBConstruct 1–249; UniProt 382–630 Author chain M; PDBConstruct 1–249; UniProt 382–630 Author chain N; PDBConstruct 1–249; UniProt 382–630 Author chain O; PDBConstruct 1–249; UniProt 382–630 Author chain P; PDBConstruct 1–249; UniProt 382–630 Author chain Q; PDBConstruct 1–249; UniProt 382–630 Author chain R; PDBConstruct 1–249; UniProt 382–630 Author chain S; PDBConstruct 1–249; UniProt 382–630 Author chain T; PDBConstruct 1–249; UniProt 382–630 Author chain V; PDBConstruct 1–249; UniProt 382–630 Author chain W; PDBConstruct 1–249; UniProt 382–630 Author chain X; PDBConstruct 1–249; UniProt 382–630 Author chain Y; PDBConstruct 1–249; UniProt 382–630

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_id8orb
Deposition date deposition_date2023-04-13
Structure title title24-meric catalytic domain of dihydrolipoamide acetyltransferase (E2) of the E. coli pyruvate dehydrogenase complex.
Keywords keywordspyruvate dehydrogenase complex, PDHc, E2, cryo-EM, TRANSFERASE; TRANSFERASE
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.

8orb__assembly_1__model_1

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

Download this curve (.dat)

8orb__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.

8orb__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)63.74 Å
Rg (electron density)62.61 Å
Total Rg62.85 Å
Atom count45984
Residues5928
Excluded volume830070 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8orb__assembly_1__model_1 24-meric (24) 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 (1)

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7. Citations (1)