9M46: IQSEC2 CC domain

Crystal structure of IQSEC2 CC domain. Determined by X-ray diffraction at 1.77 Å resolution. Released 22 Oct 2025.

Method: X-ray diffraction
Resolution: 1.77 Å
Organism: Homo sapiens
Chains: 4
Atoms: 1,883
Mol. weight: 31.39 kDa
Released: 22 Oct 2025

Explore 9M46 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9M46 contains 4 α-helices and 0 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	18-67	50

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	17-64	48

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	19-67	49

Chain D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	19-65	47

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
IQ motif and SEC7 domain-containing protein 2	A, B, C, D	protein	67	Homo sapiens	Q5JU85 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>9M46_1 IQ motif and SEC7 domain-containing protein 2 (chains A, B, C, D)
GPGSGSESPNRAVEYLLELNNIIESQQQLLETQRRRIEELEGQLDQLTQENRDLREESQL
HRGELHR

Primary citation

IQSEC2/BRAG1 may modulate postsynaptic density assembly through Ca2+-induced phase separation. Bai, G., Huang, R., Nan, X. et al. J Cell Biol (2025) 224. DOI 10.1083/jcb.202503076 · PubMed

Other PDB entries of the same protein (UniProt Q5JU85 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6FAE 2.35 Å, The Sec7 domain of IQSEC2 (Brag1) in complex with the small GTPase Arf1

Browse structure collections

About this viewer

MolViewer shows 9M46 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.