9QFG: Cofilin-1

Cryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1, strand boundary. Determined by electron microscopy at 3.49 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 3.49 Å
Organism: Homo sapiens
Chains: 14
Atoms: 38,144
Mol. weight: 705.59 kDa
Ligands: MG, ADP
Released: 8 Oct 2025

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

Secondary structure: helices and β-sheets

9QFG contains 222 α-helices and 342 β-strands across 14 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, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	53
β-strand	16-21	6	53
β-strand	29-32	4	53
β-strand	35-38	4	54
β-strand	53-54	2	54
α-helix	56-60	5
β-strand	65-68	4	54
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	53
α-helix	113-125	13
β-strand	131-136	6	53
α-helix	137-144	8
β-strand	150-155	6	55
β-strand	160-166	7	55
β-strand	169-170	2	55
α-helix	172-174	3
β-strand	176-178	3	55
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	56
β-strand	247-250	4	56
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	55
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	55
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	53
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain B: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	57
β-strand	16-21	6	57
β-strand	29-32	4	57
β-strand	35-38	4	58
β-strand	53-54	2	58
α-helix	56-60	5
β-strand	65-68	4	58
β-strand	71-72	2	59
β-strand	75-76	2	59
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	57
α-helix	113-125	13
β-strand	131-136	6	57
α-helix	137-144	8
β-strand	150-155	6	60
β-strand	160-166	7	60
β-strand	169-170	2	60
α-helix	172-174	3
β-strand	176-178	3	60
α-helix	182-193	12
α-helix	194-196	3
α-helix	204-216	13
α-helix	223-232	10
β-strand	238-241	4	61
β-strand	247-250	4	61
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	60
α-helix	302-304	3
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	60
α-helix	335-337	3
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	57
α-helix	359-365	7
α-helix	368-371	4

Chain C: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	62
β-strand	16-21	6	62
β-strand	29-32	4	62
β-strand	35-38	4	63
β-strand	53-54	2	63
α-helix	56-60	5
β-strand	65-68	4	63
β-strand	71-72	2	64
β-strand	75-76	2	64
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	62
α-helix	113-125	13
β-strand	131-136	6	62
α-helix	137-144	8
β-strand	150-155	6	65
β-strand	160-166	7	65
β-strand	169-170	2	65
α-helix	172-174	3
β-strand	176-178	3	65
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	66
β-strand	247-250	4	66
α-helix	253-256	4
α-helix	258-261	4
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	65
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	65
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	62
α-helix	359-365	7
α-helix	368-371	4

Chain D: 26 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	67
β-strand	16-21	6	67
β-strand	29-32	4	67
β-strand	35-38	4	68
β-strand	41-42	2	60
β-strand	53-54	2	68
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	68
β-strand	71-72	2	69
β-strand	75-76	2	69
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	67
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	67
α-helix	137-144	8
β-strand	150-155	6	70
β-strand	160-166	7	70
β-strand	169-170	2	70
α-helix	172-174	3
β-strand	176-178	3	70
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	71
β-strand	247-250	4	71
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	70
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	70
α-helix	335-337	3
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	67
α-helix	359-365	7
α-helix	368-371	4

Chain E: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	72
β-strand	16-21	6	72
β-strand	29-32	4	72
β-strand	35-38	4	73
β-strand	41-42	2	65
β-strand	53-54	2	73
α-helix	56-60	5
β-strand	65-68	4	73
β-strand	71-72	2	74
β-strand	75-76	2	74
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	72
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	72
α-helix	137-144	8
β-strand	150-155	6	75
β-strand	160-166	7	75
β-strand	169-170	2	75
α-helix	172-174	3
β-strand	176-178	3	75
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	76
β-strand	247-250	4	76
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	75
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	75
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	72
α-helix	359-365	7
α-helix	368-371	4

Chain F: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	77
β-strand	16-21	6	77
β-strand	29-32	4	77
β-strand	35-38	4	78
β-strand	42	1	70
β-strand	53-54	2	78
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	78
β-strand	71-72	2	79
β-strand	75-76	2	79
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	77
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	77
α-helix	137-144	8
β-strand	150-155	6	80
β-strand	160-166	7	80
β-strand	169-170	2	80
α-helix	172-174	3
β-strand	176-178	3	80
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	81
β-strand	247-250	4	81
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	80
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	80
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	77
α-helix	359-365	7
α-helix	368-371	4

Chain G: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	82
β-strand	16-21	6	82
β-strand	29-32	4	82
β-strand	35-38	4	83
β-strand	42	1	75
β-strand	53-54	2	83
α-helix	56-59	4
α-helix	62-64	3
β-strand	65-68	4	83
β-strand	71-72	2	84
β-strand	75-76	2	84
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	82
α-helix	113-125	13
β-strand	131-136	6	82
α-helix	137-144	8
β-strand	150-155	6	85
β-strand	160-166	7	85
β-strand	169-170	2	85
α-helix	172-174	3
β-strand	176-178	3	85
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	86
β-strand	247-250	4	86
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	85
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	85
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	82
α-helix	359-365	7
α-helix	368-371	4

Chain H: 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	67-73	7
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

6 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	H, I	protein	166	Homo sapiens	P23528 (AlphaFold model)
Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase	J, K, L, M, N	protein	688	Homo sapiens	P16455 (AlphaFold model), Q9BR76 (AlphaFold model)
Actin, cytoplasmic 1, N-terminally processed	A, B, C, D, E, F, G	protein	374	Homo sapiens	P60709 (AlphaFold model)

Sequence of entity 1 (H, I), FASTA

>9QFG_1 Cofilin-1 (chains H, I)
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDV
GQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS
KDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

Sequence of entity 2 (J, K, L, M, N), FASTA

>9QFG_2 Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase (chains J, K, L, M, N)
GAMGSMSFRKVVRQSKFRHVFGQPVKNDQCYEDIRVSRVTWDSTFCAVNPKFLAVIVEAS
GGGAFLVLPLSKTGRIDKAYPTVCGHTGPVLDIDWCPHNDEVIASGSEDCTVMVWQIPEN
GLTSPLTEPVVVLEGHTKRVGIIAWHPTARNVLLSAGCDNVVLIWNVGTAEELYRLDSLH
PDLIYNVSWNHNGSLFCSACKDKSVRIIDPRRGTLVAEREKAHEGARPMRAIFLADGKVF
TTGFSRMSERQLALWDPENLEEPMALQELDSSNGALLPFYDPDTSVVYVCGKGDSSIRYF
EITEEPPYIHFLNTFTSKEPQRGMGSMPKRGLEVSKCEIARFYKLHERKCEPIVMTVPRK
SDLFQDDLYPDTAGPEAALEAEEWVSGRDADPILISLREAYVPSKQRDLKISRRNVLSDS
RPAMAPGSSHLGAPASTTTAADATPSGSLARAGEAGKLEEVMQELRALRALVKEQGDRIC
RLEEQLGRMENGDAGTGGGGSGGGGSMDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLL
GKGTSAADAVEVPAPAAVLGGPEPLMQATAWLNAYFHQPEAIEEFPVPALHHPVFQQESF
TRQVLWKLLKVVKFGEVISYQQLAALAGNPAATAAVKTALSGNPVPILIPCHRVVSSSGA
VGGYEGGLAVKEWLLAHEGHRLGKPGLG

Sequence of entity 3 (A, B, C, D, E, F, G), FASTA

>9QFG_3 Actin, cytoplasmic 1, N-terminally processed (chains A, B, C, D, E, F, G)
DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK
RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ
IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA
GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE
LPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVLSG
GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE
YDESGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	7
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	7

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
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
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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