9H1F: Cofilin-1

Cofilin-1 in complex with high-affinity Sybody B12. Determined by X-ray diffraction at 1.8 Å resolution. Released 19 Mar 2025.

Method: X-ray diffraction
Resolution: 1.8 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 2,284
Mol. weight: 31.79 kDa
Released: 19 Mar 2025

Explore 9H1F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9H1F contains 11 α-helices and 20 β-strands across 2 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: 9 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	13-14	2	1
α-helix	15	1
α-helix	16-25	10
α-helix	33-37	5
β-strand	40-47	8	1
β-strand	53-63	11	1
α-helix	64-66	3
β-strand	67	1	2
β-strand	71	1	2
α-helix	74-81	8
β-strand	88-97	10	1
β-strand	102-111	10	1
α-helix	118-134	17
β-strand	141-144	4	1
α-helix	147-150	4
α-helix	153-161	9
α-helix	162-164	3
β-strand	167-168	2	1
β-strand	171-172	2	1

Chain B: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	5-9	5	3
β-strand	12-15	4	4
β-strand	20-27	8	3
α-helix	31-33	3
β-strand	36-41	6	4
β-strand	48-53	6	4
β-strand	60-62	3	4
β-strand	70-75	6	3
β-strand	80-85	6	3
α-helix	90-92	3
β-strand	94-100	7	4
β-strand	110-115	6	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cofilin-1	A	protein	173	Homo sapiens	P23528 (AlphaFold model)
SybodyB12	B	protein	116	synthetic construct

Sequence of entity 1 (A), FASTA

>9H1F_1 Cofilin-1 (chains A)
SNIGSGSMASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGK
EILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKS
KMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

Sequence of entity 2 (B), FASTA

>9H1F_2 SybodyB12 (chains B)
GHQVQLVESGGGLVQAGGSLRLSCAASGFPVNHRTMAWYRQAPGKEREWVAAIESHGQET
WYADSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCVRVGAEYVGQGTQVTVSA

Primary citation

A high affinity Sybody blocks Cofilin-1 binding to F-actin in vitro and in cancer cells. Paraschiakos, T., Li, J., Scholz, J. et al. Biochem Pharmacol (2025) 236:116866-116866. DOI 10.1016/j.bcp.2025.116866 · PubMed

Other PDB entries of the same protein (UniProt P23528 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9QFJ 2.31 Å, Cryo-EM structure of the cofilactin filament core at 2.3 Angstrom resolution.
5L6W 2.53 Å, Structure Of the LIMK1-ATPgammaS-CFL1 Complex
9QFD 2.61 Å, Cryo-EM structure of the fully cofilin-1-decorated actin filament (cofilactin)
9QFQ 2.76 Å, Cryo-EM structure of the cofilactin barbed end bound by AIP1
4BEX 2.8 Å, Structure of human Cofilin1
9QFO 2.96 Å, Cryo-EM structure of the cofilactin filament pointed end
9QFE 3.12 Å, Cryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on…
9QFW 3.16 Å, Cryo-EM structure of the cofilactin barbed end bound by two AIP1 molecules
6VAO 3.4 Å, Human cofilin-1 decorated actin filament
9QFG 3.49 Å, Cryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1,…
5HVK 3.5 Å, Crystal structure of LIMK1 mutant D460N in complex with full-length cofilin-1
9QFK 3.99 Å, Cryo-EM structure of the Coronin-1B-decorated actin filament bound by one Cofilin-1…

Browse structure collections

About this viewer

MolViewer shows 9H1F 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.