9QFO: Cofilactin filament pointed end

Cryo-EM structure of the cofilactin filament pointed end. Determined by electron microscopy at 2.96 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 2.96 Å
Organism: Homo sapiens
Chains: 10
Atoms: 22,156
Mol. weight: 326.63 kDa
Ligands: ADP, MG
Released: 8 Oct 2025

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

Secondary structure: helices and β-sheets

9QFO contains 184 α-helices and 150 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: 23 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	13
β-strand	16-21	6	13
β-strand	29-32	4	13
β-strand	35-38	4	14
β-strand	53-54	2	14
α-helix	56-60	5
β-strand	65-68	4	14
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	13
α-helix	113-125	13
β-strand	131-136	6	13
α-helix	137-144	8
β-strand	150-155	6	15
β-strand	160-166	7	15
β-strand	169-170	2	15
α-helix	172-174	3
β-strand	176-178	3	15
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-240	3	16
β-strand	248-250	3	16
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	15
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	15
α-helix	335-337	3
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	13
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain B: 25 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	17
β-strand	16-21	6	17
β-strand	29-32	4	17
β-strand	35-38	4	18
β-strand	53-54	2	18
α-helix	56-60	5
β-strand	65-68	4	18
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	17
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	17
α-helix	137-144	8
β-strand	150-155	6	19
β-strand	160-166	7	19
β-strand	169-170	2	19
α-helix	172-174	3
β-strand	176-178	3	19
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	20
β-strand	247-250	4	20
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	19
α-helix	302-304	3
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	19
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	17
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain C: 22 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	21
β-strand	16-21	6	21
β-strand	29-32	4	21
β-strand	35-38	4	22
β-strand	53-54	2	22
α-helix	56-60	5
β-strand	65-68	4	22
α-helix	79-87	9
α-helix	88-93	6
β-strand	96	1	2
α-helix	98-100	3
β-strand	103-107	5	21
α-helix	113-125	13
β-strand	131-136	6	21
α-helix	137-144	8
β-strand	150-155	6	23
β-strand	160-166	7	23
β-strand	169-170	2	23
α-helix	172-174	3
β-strand	176-178	3	23
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	24
β-strand	247-250	4	24
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	23
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	23
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	21
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain D: 26 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	25
β-strand	16-21	6	25
β-strand	29-32	4	25
β-strand	35-38	4	26
β-strand	53-54	2	26
α-helix	56-60	5
β-strand	65-68	4	26
α-helix	79-87	9
α-helix	88-93	6
β-strand	96	1	5
α-helix	98-100	3
β-strand	103-107	5	25
α-helix	113-125	13
β-strand	131-136	6	25
α-helix	137-144	8
β-strand	150-155	6	27
β-strand	160-166	7	27
β-strand	169-170	2	27
α-helix	172-174	3
β-strand	176-178	3	27
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	28
β-strand	247-250	4	28
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	27
α-helix	302-304	3
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	27
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	25
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain E: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	29
β-strand	16-21	6	29
β-strand	29-32	4	29
β-strand	35-38	4	30
β-strand	53-54	2	30
α-helix	56-60	5
β-strand	65-68	4	30
α-helix	79-87	9
α-helix	88-93	6
β-strand	96	1	8
β-strand	103-107	5	29
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	29
α-helix	137-144	8
β-strand	150-155	6	31
β-strand	160-166	7	31
β-strand	169-170	2	31
α-helix	172-174	3
β-strand	176-178	3	31
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	32
β-strand	247-250	4	32
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	31
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	31
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	29
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain F: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	33
β-strand	16-21	6	33
β-strand	29-32	4	33
β-strand	35-38	4	34
β-strand	53-54	2	34
α-helix	56-60	5
β-strand	65-68	4	34
α-helix	79-87	9
α-helix	88-93	6
β-strand	96	1	11
α-helix	98-100	3
β-strand	103-107	5	33
α-helix	113-125	13
β-strand	131-136	6	33
α-helix	137-144	8
β-strand	150-155	6	35
β-strand	160-166	7	35
β-strand	169-170	2	35
α-helix	172-174	3
β-strand	176-178	3	35
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	36
β-strand	247-250	4	36
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-295	9
β-strand	297-300	4	35
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	35
α-helix	335-337	3
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	33
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain G: 10 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	5	1
β-strand	6-7	2	1
α-helix	8	1
α-helix	9-19	11
β-strand	21	1	2
α-helix	22-23	2
α-helix	26-29	4
β-strand	33-40	8	1
β-strand	46-56	11	1
β-strand	60	1	3
β-strand	64	1	3
α-helix	67-74	8
β-strand	81-91	11	1
β-strand	95-104	10	1
α-helix	111-127	17
β-strand	133-137	5	1
α-helix	141-144	4
α-helix	146-154	9
α-helix	155-157	3
β-strand	158-161	4	1
β-strand	164-165	2	1

Chain H: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	4
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
β-strand	60	1	6
β-strand	64	1	6
α-helix	67-74	8
β-strand	81-91	11	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	146-153	8
α-helix	155-157	3
β-strand	158-161	4	4
β-strand	164-165	2	4

2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

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

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

>9QFO_1 Cofilin-1 (chains G, H, I, J)
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDV
GQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS
KDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

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

>9QFO_2 Actin, cytoplasmic 1, N-terminally processed (chains A, B, C, D, E, F)
DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK
RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ
IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA
GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE
LPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVLSG
GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE
YDESGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6
MG	Magnesium ion	Mg	6

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
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
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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