7og1

AP2 clathrin adaptor core in complex with cargo peptide and FCHO2

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

AP-2 complex subunit alpha-2

Rattus norvegicus

UniProt P18484

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit mu × 2 (P84092) AP-2 complex subunit sigma × 1 (P62743) F-BAR domain only protein 2 × 2 (Q0JRZ9) TGN38 CARGO PEPTIDE × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP2A2_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 1–621; UniProt 1–620

AP-2 complex subunit beta

Homo sapiens

UniProt P63010

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-2 complex subunit alpha-2 × 1 (P18484) AP-2 complex subunit mu × 2 (P84092) AP-2 complex subunit sigma × 1 (P62743) F-BAR domain only protein 2 × 2 (Q0JRZ9) TGN38 CARGO PEPTIDE × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP2B1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain BBB; PDBConstruct 1–591; UniProt 1–591

AP-2 complex subunit mu

Rattus norvegicus

UniProt P84092

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-2 complex subunit alpha-2 × 1 (P18484) AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit sigma × 1 (P62743) F-BAR domain only protein 2 × 2 (Q0JRZ9) TGN38 CARGO PEPTIDE × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP2M1_RAT
Isoform —
PDB entities 3
Chains and sequence ranges Author chain CCC; PDBConstruct 1–446; UniProt 1–435 Author chain MMM; PDBConstruct 1–446; UniProt 1–435

AP-2 complex subunit sigma

Mus musculus

UniProt P62743

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-2 complex subunit alpha-2 × 1 (P18484) AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit mu × 2 (P84092) F-BAR domain only protein 2 × 2 (Q0JRZ9) TGN38 CARGO PEPTIDE × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP2S1_MOUSE
Isoform —
PDB entities 4
Chains and sequence ranges Author chain SSS; PDBConstruct 1–142; UniProt 1–142

F-BAR domain only protein 2

Homo sapiens

UniProt Q0JRZ9

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-2 complex subunit alpha-2 × 1 (P18484) AP-2 complex subunit beta × 1 (P63010) AP-2 complex subunit mu × 2 (P84092) AP-2 complex subunit sigma × 1 (P62743) TGN38 CARGO PEPTIDE × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name FCHO2_HUMAN
Isoform —
PDB entities 5
Chains and sequence ranges Author chain DDD; PDBConstruct 6–136; UniProt 314–444 Author chain GGG; PDBConstruct 6–136; UniProt 314–444

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_id7og1
Deposition date deposition_date2021-05-05
Structure title titleAP2 clathrin adaptor core in complex with cargo peptide and FCHO2
Keywords keywordsclathrin-mediated endocytosis (CME), protein recycling, plasma membrane, ENDOCYTOSIS; ENDOCYTOSIS
Experimental Method methodX-RAY DIFFRACTION
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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.

7og1__assembly_1__model_1

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

Download this curve (.dat)

7og1__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.

7og1__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)39.69 Å
Rg (electron density)38.64 Å
Total Rg39.18 Å
Atom count14391
Residues1804
Excluded volume258830 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 7og1__assembly_1__model_1 octameric (8) 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 (6)

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7. Citations (2)