› 5h3d

Electron Microscopy
14Å resolution

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

Released:
DOI: 10.2210/pdb5h3d/pdb
PDB entry 5h3d coloured by chain, front view.
PDB entry 5h3d coloured by chain, side view.
PDB entry 5h3d coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages.
Chan C, Pang X, Zhang Y, Niu T, Yang S, Zhao D, Li J, Lu L, Hsu VW, Zhou J, Sun F, Fan J
OpenAccess logo PLoS Comput Biol 15 e1007081 (2019)
PMID: 31291238
Related structures: EMD-2546

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo 36-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 382 amino acids
Theoretical weight: 43.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15027 (Residues: 1-377; Coverage: 51%)
Gene names: ACAP1, CENTB1, KIAA0050
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 14Å
Relevant EMDB volumes: EMD-2546
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Creativity comes from interactions: modules of protein interactions in plants.
Allen et al. (2022)

1 mention without citation

ACAP1 assembles into an unusual protein lattice for membrane deformation through multiple stages.
Chan et al. (2019)