9u9j

M4-CTD-docked AP-4 core in apo form

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

AP-4 complex subunit beta-1

Homo sapiens

UniProt Q9Y6B7

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 AP-4 complex subunit epsilon-1 × 1 (Q9UPM8) AP-4 complex subunit mu-1 × 1 (O00189) AP-4 complex subunit sigma-1 × 1 (Q9Y587) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP4B1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–568; UniProt 1–568

AP-4 complex subunit epsilon-1

Homo sapiens

UniProt Q9UPM8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 AP-4 complex subunit beta-1 × 1 (Q9Y6B7) AP-4 complex subunit mu-1 × 1 (O00189) AP-4 complex subunit sigma-1 × 1 (Q9Y587) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP4E1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–612; UniProt 1–612

AP-4 complex subunit mu-1

Homo sapiens

UniProt O00189

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 AP-4 complex subunit beta-1 × 1 (Q9Y6B7) AP-4 complex subunit epsilon-1 × 1 (Q9UPM8) AP-4 complex subunit sigma-1 × 1 (Q9Y587) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP4M1_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain M; PDBConstruct 1–453; UniProt 1–453

AP-4 complex subunit sigma-1

Homo sapiens

UniProt Q9Y587

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 AP-4 complex subunit beta-1 × 1 (Q9Y6B7) AP-4 complex subunit epsilon-1 × 1 (Q9UPM8) AP-4 complex subunit mu-1 × 1 (O00189) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP4S1_HUMAN
Isoform —
PDB entities 4
Chains and sequence ranges Author chain S; PDBConstruct 1–144; UniProt 1–144

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_id9u9j
Deposition date deposition_date2025-03-28
Structure title titleM4-CTD-docked AP-4 core in apo form
Keywords keywordsAP-4 complex, PROTEIN TRANSPORT; PROTEIN 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.

9u9j__assembly_1__model_1

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

Download this curve (.dat)

9u9j__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.

9u9j__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)41.37 Å
Rg (electron density)40.80 Å
Total Rg41.30 Å
Atom count12243
Residues1529
Excluded volume220590 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9u9j__assembly_1__model_1 tetrameric (4) 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 (4)

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7. Citations (1)