9FJN: Inverted formin-2

Solution NMR structure of a peptide encompassing residues 2-19 of the human formin INF2. Determined by solution NMR. Released 11 Sept 2024.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 140
Mol. weight: 2 kDa
Released: 11 Sept 2024

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

Secondary structure: helices and β-sheets

9FJN contains 1 α-helix and 0 β-strands across 1 chain. 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	2-16	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Inverted formin-2	A	protein	18	Homo sapiens	Q27J81 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9FJN_1 Inverted formin-2 (chains A)
SVKEGAQRKWAALKEKLG

Primary citation

Structure and function of the N-terminal extension of the formin INF2. Labat-de-Hoz, L., Comas, L., Rubio-Ramos, A. et al. Cell Mol Life Sci (2022) 79:571. DOI 10.1016/j.jmb.2015.09.014 · PubMed

Other PDB entries of the same protein (UniProt Q27J81 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9B03 2.95 Å, INF2 in the Middle of F-Actin (Up state)
9B0K 3.03 Å, INF2 in the Middle of F-Actin (Down state)
9AZ4 3.37 Å, INF2 at the Barbed End of F-Actin
8RV2 3.41 Å, Structure of the formin INF2 bound to the barbed end of F-actin.
9AZP 3.79 Å, INF2 at the Barbed End of F-Actin with Incoming Profilin-Actin
9AZQ 3.82 Å, INF2 at the Barbed End of F-Actin with Incoming Actin
9FJW Solution NMR structure of a peptide encompassing residues 2-36 of the human formin INF2
9G7T Solution NMR structure of a peptide encompassing residues 967-991 of the human formin INF2
9RWF Solution NMR structure of a peptide encompassing residues 967-991 of the human formin INF2

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