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5h3d

Helical structure of membrane tubules decorated by ACAP1 (BARPH doamin) protein by cryo-electron microscopy and MD simulation

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

Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1

Homo sapiens

UniProt Q15027

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 36 No other associated polymer Consistent with protein count
2 Protein homooligomer Homooligomer Protein 4 No other associated polymer Consistent with protein count
3 Protein homooligomer Homooligomer Protein 4 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

Monomer
3jue 3jue 4f1p 4f1p

4 assemblies

Homodimer
4nsw

1 assemblies

Homotetramer
5h3d 5h3d

2 assemblies

Other homooligomers
4ckg 4ckh 5h3d

3 assemblies

Heteromeric or nucleic-acid complex
3t9k 3t9k

2 assemblies

View Construct and Data Evidence
UniProt name ACAP1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 6–382； UniProt 1–377 Author chain B； PDBConstruct 6–382； UniProt 1–377 Author chain C； PDBConstruct 6–382； UniProt 1–377 Author chain D； PDBConstruct 6–382； UniProt 1–377

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_id5h3d
Deposition date deposition_date2016-10-22
Structure title titleHelical structure of membrane tubules decorated by ACAP1 (BARPH doamin) protein by cryo-electron microscopy and MD simulation
Keywords keywordsACAP1 BARPH domain, membrane remodeling, molecular dynamics simulation, SIGNALING PROTEIN; SIGNALING PROTEIN
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.

5h3d__assembly_1__model_1

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

Download this curve (.dat)

5h3d__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 108 109 1010 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

5h3d__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）0.00 Å
Rg (electron density)190.20 Å
Total Rg190.30 Å
Atom count209826
Residues13050
Excluded volume1854000 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5h3d__assembly_1__model_1 36-meric （36） Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 5h3d__assembly_2__model_1 tetrameric （4） Excluded — —
Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
3 1 5h3d__assembly_3__model_1 tetrameric （4） Excluded — —
Exclusion reason： Auxiliary symmetry representation; not a complete or representative biological assembly.
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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)