9QFJ: Cofilactin filament core

Cryo-EM structure of the cofilactin filament core at 2.3 Angstrom resolution. Determined by electron microscopy at 2.31 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 2.31 Å
Organism: Homo sapiens
Chains: 10
Atoms: 21,467
Mol. weight: 303.08 kDa
Ligands: MG, ADP
Released: 8 Oct 2025

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

Secondary structure: helices and β-sheets

9QFJ contains 185 α-helices and 143 β-strands across 10 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: 25 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	15
β-strand	16-21	6	15
β-strand	29-32	4	15
β-strand	35-38	4	16
β-strand	53-54	2	16
α-helix	56-60	5
β-strand	65-68	4	16
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	15
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	15
α-helix	137-144	8
β-strand	150-155	6	17
β-strand	160-166	7	17
β-strand	169-170	2	17
α-helix	172-174	3
β-strand	176-178	3	17
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	18
β-strand	247-250	4	18
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	17
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	17
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	15
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chains B, C, D and E: 25 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	19
β-strand	16-21	6	19
β-strand	29-32	4	19
β-strand	35-38	4	20
β-strand	53-54	2	20
α-helix	56-60	5
β-strand	65-68	4	20
α-helix	79-88	10
α-helix	89-93	5
β-strand	96	1	5
α-helix	98-100	3
β-strand	103-107	5	19
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	19
α-helix	137-144	8
β-strand	150-155	6	21
β-strand	160-166	7	21
β-strand	169-170	2	21
α-helix	172-174	3
β-strand	176-178	3	21
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	22
β-strand	247-250	4	22
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	21
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	21
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	19
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chains F, G, H and I: 12 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	5	1
β-strand	6-7	2	4
α-helix	8	1
α-helix	9-19	11
β-strand	21	1	5
α-helix	22-23	2
α-helix	26-29	4
β-strand	33-40	8	4
β-strand	46-56	11	4
α-helix	57-59	3
β-strand	60	1	6
β-strand	64	1	6
α-helix	67-74	8
β-strand	81-90	10	4
β-strand	95-104	10	4
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-137	5	4
α-helix	140-142	3
α-helix	146-154	9
α-helix	155-157	3
β-strand	160-161	2	4
β-strand	164-165	2	4

Chain J: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	5	1
β-strand	6-7	2	13
α-helix	8	1
α-helix	9-19	11
α-helix	21-23	3
α-helix	26-29	4
β-strand	33-40	8	13
β-strand	46-56	11	13
α-helix	57-59	3
β-strand	60	1	14
β-strand	64	1	14
α-helix	67-74	8
β-strand	81-90	10	13
β-strand	95-104	10	13
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-137	5	13
α-helix	140-142	3
α-helix	146-154	9
α-helix	155-157	3
β-strand	160-161	2	13
β-strand	164-165	2	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cofilin-1	F, G, H, I, J	protein	166	Homo sapiens	P23528 (AlphaFold model)
Actin, cytoplasmic 1, N-terminally processed	A, B, C, D, E	protein	374	Homo sapiens	P60709 (AlphaFold model)

Sequence of entity 1 (F, G, H, I, J), FASTA

>9QFJ_1 Cofilin-1 (chains F, G, H, I, J)
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDV
GQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS
KDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

Sequence of entity 2 (A, B, C, D, E), FASTA

>9QFJ_2 Actin, cytoplasmic 1, N-terminally processed (chains A, B, C, D, E)
DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK
RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ
IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA
GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE
LPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVLSG
GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE
YDESGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	5
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	5

Primary citation

Choreography of rapid actin filament disassembly by coronin, cofilin, and AIP1. Oosterheert, W., Boiero Sanders, M., Hofnagel, O. et al. Cell (2025) 188:6845. DOI 10.1016/j.cell.2025.09.016 · PubMed

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

9H1F 1.8 Å, Cofilin-1 in complex with high-affinity Sybody B12
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…

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