9rtw

Mammalian AP3 complex on tubular membranes (AP3 centered)

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

AP-3 complex subunit beta

Pan troglodytes

UniProt A0A2I3SW12

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-3 complex subunit delta-1 × 1 (O14617) ADP-ribosylation factor 1 × 4 (P84077) AP-3 complex subunit mu-1 × 1 (A6KKR5) AP-3 complex subunit sigma-1 × 1 (Q92572) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A2I3SW12_PANTR
Isoform —
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–563; UniProt 43–636

AP-3 complex subunit delta-1

Homo sapiens

UniProt O14617

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-3 complex subunit beta × 1 (A0A2I3SW12) ADP-ribosylation factor 1 × 4 (P84077) AP-3 complex subunit mu-1 × 1 (A6KKR5) AP-3 complex subunit sigma-1 × 1 (Q92572) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP3D1_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–615; UniProt 18–632

ADP-ribosylation factor 1

Homo sapiens

UniProt P84077

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-3 complex subunit beta × 1 (A0A2I3SW12) AP-3 complex subunit delta-1 × 1 (O14617) AP-3 complex subunit mu-1 × 1 (A6KKR5) AP-3 complex subunit sigma-1 × 1 (Q92572) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name ARF1_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–167; UniProt 15–181 Author chain F; PDBConstruct 1–167; UniProt 15–181 Author chain G; PDBConstruct 1–167; UniProt 15–181 Author chain H; PDBConstruct 1–167; UniProt 15–181

AP-3 complex subunit mu-1

Rattus norvegicus

UniProt A6KKR5

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-3 complex subunit beta × 1 (A0A2I3SW12) AP-3 complex subunit delta-1 × 1 (O14617) ADP-ribosylation factor 1 × 4 (P84077) AP-3 complex subunit sigma-1 × 1 (Q92572) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A6KKR5_RAT
Isoform —
PDB entities 4
Chains and sequence ranges Author chain M; PDBConstruct 1–418; UniProt 1–418

AP-3 complex subunit sigma-1

Homo sapiens

UniProt Q92572

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 8 AP-3 complex subunit beta × 1 (A0A2I3SW12) AP-3 complex subunit delta-1 × 1 (O14617) ADP-ribosylation factor 1 × 4 (P84077) AP-3 complex subunit mu-1 × 1 (A6KKR5) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name AP3S1_HUMAN
Isoform —
PDB entities 5
Chains and sequence ranges Author chain S; PDBConstruct 1–153; UniProt 1–153

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_id9rtw
Deposition date deposition_date2025-07-03
Structure title titleMammalian AP3 complex on tubular membranes (AP3 centered)
Keywords keywordsCargo adapter, Coat, trafficking, ENDOCYTOSIS; ENDOCYTOSIS
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.

9rtw__assembly_1__model_1

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

Download this curve (.dat)

9rtw__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.

9rtw__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)52.38 Å
Rg (electron density)52.41 Å
Total Rg52.44 Å
Atom count9669
Residues2417
Excluded volume133150 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 9rtw__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 (5)

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7. Citations (1)