8piu

60-meric complex of dihydrolipoamide acetyltransferase (E2) of the human pyruvate dehydrogenase complex

Method: ELECTRON MICROSCOPY

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

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial

Homo sapiens

UniProt P10515

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 60 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_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–562; UniProt 87–647 Author chain AA; PDBConstruct 2–562; UniProt 87–647 Author chain AB; PDBConstruct 2–562; UniProt 87–647 Author chain B; PDBConstruct 2–562; UniProt 87–647 Author chain BA; PDBConstruct 2–562; UniProt 87–647 Author chain BB; PDBConstruct 2–562; UniProt 87–647 Author chain C; PDBConstruct 2–562; UniProt 87–647 Author chain CA; PDBConstruct 2–562; UniProt 87–647 Author chain CB; PDBConstruct 2–562; UniProt 87–647 Author chain D; PDBConstruct 2–562; UniProt 87–647 Author chain DA; PDBConstruct 2–562; UniProt 87–647 Author chain DB; PDBConstruct 2–562; UniProt 87–647 Author chain E; PDBConstruct 2–562; UniProt 87–647 Author chain EA; PDBConstruct 2–562; UniProt 87–647 Author chain EB; PDBConstruct 2–562; UniProt 87–647 Author chain F; PDBConstruct 2–562; UniProt 87–647 Author chain FA; PDBConstruct 2–562; UniProt 87–647 Author chain FB; PDBConstruct 2–562; UniProt 87–647 Author chain G; PDBConstruct 2–562; UniProt 87–647 Author chain GA; PDBConstruct 2–562; UniProt 87–647 Author chain GB; PDBConstruct 2–562; UniProt 87–647 Author chain H; PDBConstruct 2–562; UniProt 87–647 Author chain HA; PDBConstruct 2–562; UniProt 87–647 Author chain HB; PDBConstruct 2–562; UniProt 87–647 Author chain I; PDBConstruct 2–562; UniProt 87–647 Author chain IA; PDBConstruct 2–562; UniProt 87–647 Author chain IB; PDBConstruct 2–562; UniProt 87–647 Author chain J; PDBConstruct 2–562; UniProt 87–647 Author chain JA; PDBConstruct 2–562; UniProt 87–647 Author chain K; PDBConstruct 2–562; UniProt 87–647 Author chain KA; PDBConstruct 2–562; UniProt 87–647 Author chain L; PDBConstruct 2–562; UniProt 87–647 Author chain LA; PDBConstruct 2–562; UniProt 87–647 Author chain M; PDBConstruct 2–562; UniProt 87–647 Author chain MA; PDBConstruct 2–562; UniProt 87–647 Author chain N; PDBConstruct 2–562; UniProt 87–647 Author chain NA; PDBConstruct 2–562; UniProt 87–647 Author chain O; PDBConstruct 2–562; UniProt 87–647 Author chain OA; PDBConstruct 2–562; UniProt 87–647 Author chain P; PDBConstruct 2–562; UniProt 87–647 Author chain PA; PDBConstruct 2–562; UniProt 87–647 Author chain Q; PDBConstruct 2–562; UniProt 87–647 Author chain QA; PDBConstruct 2–562; UniProt 87–647 Author chain R; PDBConstruct 2–562; UniProt 87–647 Author chain RA; PDBConstruct 2–562; UniProt 87–647 Author chain S; PDBConstruct 2–562; UniProt 87–647 Author chain SA; PDBConstruct 2–562; UniProt 87–647 Author chain T; PDBConstruct 2–562; UniProt 87–647 Author chain TA; PDBConstruct 2–562; UniProt 87–647 Author chain UA; PDBConstruct 2–562; UniProt 87–647 Author chain V; PDBConstruct 2–562; UniProt 87–647 Author chain VA; PDBConstruct 2–562; UniProt 87–647 Author chain W; PDBConstruct 2–562; UniProt 87–647 Author chain WA; PDBConstruct 2–562; UniProt 87–647 Author chain X; PDBConstruct 2–562; UniProt 87–647 Author chain XA; PDBConstruct 2–562; UniProt 87–647 Author chain Y; PDBConstruct 2–562; UniProt 87–647 Author chain YA; PDBConstruct 2–562; UniProt 87–647 Author chain Z; PDBConstruct 2–562; UniProt 87–647 Author chain ZA; PDBConstruct 2–562; UniProt 87–647

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_id8piu
Deposition date deposition_date2023-06-22
Structure title title60-meric complex of dihydrolipoamide acetyltransferase (E2) of the human pyruvate dehydrogenase complex
Keywords keywordspyruvate dehydrogenase complex, PDHc, E2, cryo-EM, TRANSFERASE; TRANSFERASE
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.

8piu__assembly_1__model_1

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

Download this curve (.dat)

8piu__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 1010 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

8piu__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)99.46 Å
Rg (electron density)97.60 Å
Total Rg97.58 Å
Atom count106140
Residues13860
Excluded volume1914900 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 8piu__assembly_1__model_1 60-meric (60) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (1)

7. Citations (1)