9QFQ: Cofilactin barbed end bound by AIP1

Cryo-EM structure of the cofilactin barbed end bound by AIP1. Determined by electron microscopy at 2.76 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 2.76 Å
Organism: Homo sapiens
Chains: 11
Atoms: 25,094
Mol. weight: 389.84 kDa
Ligands: ADP, MG
Released: 8 Oct 2025

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

Secondary structure: helices and β-sheets

9QFQ contains 168 α-helices and 205 β-strands across 11 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: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	27
β-strand	16-21	6	27
β-strand	29-32	4	27
β-strand	35-38	4	28
β-strand	53-54	2	28
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	28
β-strand	71-73	3	29
β-strand	75-76	2	29
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	27
α-helix	113-125	13
β-strand	131-136	6	27
α-helix	137-144	8
β-strand	150-155	6	30
β-strand	160-166	7	30
β-strand	169-170	2	30
α-helix	172-174	3
β-strand	176-178	3	30
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	31
β-strand	247-250	4	31
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	30
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	30
α-helix	335-337	3
α-helix	338-347	10
α-helix	352-354	3
β-strand	357-358	2	27
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain B: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	32
β-strand	16-21	6	32
β-strand	29-32	4	32
β-strand	35-38	4	33
β-strand	53-54	2	33
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	33
β-strand	71	1	34
β-strand	76	1	34
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	32
α-helix	113-125	13
β-strand	131-136	6	32
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	223-231	9
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	274-282	9
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	35
α-helix	302-304	3
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	35
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	32
α-helix	359-365	7
α-helix	369-373	5

Chain C: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	37
β-strand	16-21	6	37
β-strand	29-32	4	37
β-strand	35-38	4	38
β-strand	53-54	2	38
α-helix	56-59	4
α-helix	62-64	3
β-strand	65-68	4	38
β-strand	71-73	3	39
β-strand	75-76	2	39
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	37
α-helix	113-125	13
β-strand	131-136	6	37
α-helix	137-144	8
β-strand	150-155	6	40
β-strand	160-166	7	40
β-strand	169-170	2	40
α-helix	172-174	3
β-strand	176-178	3	40
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	41
β-strand	247-250	4	41
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-282	9
α-helix	287-294	8
β-strand	297-300	4	40
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	40
α-helix	335-337	3
α-helix	338-348	11
β-strand	357-358	2	37
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain D: 26 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	42
β-strand	16-21	6	42
β-strand	29-32	4	42
β-strand	35-38	4	43
β-strand	53-54	2	43
α-helix	56-59	4
α-helix	62-64	3
β-strand	65-68	4	43
β-strand	71	1	44
β-strand	76	1	44
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	42
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	42
α-helix	137-144	8
β-strand	150-155	6	45
β-strand	160-166	7	45
β-strand	169-170	2	45
α-helix	172-174	3
β-strand	176-178	3	45
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	46
β-strand	247-250	4	46
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	287-294	8
β-strand	297-300	4	45
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	45
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	42
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain E: 26 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	47
β-strand	16-21	6	47
β-strand	29-32	4	47
β-strand	35-38	4	48
β-strand	53-54	2	48
α-helix	56-59	4
α-helix	62-64	3
β-strand	65-68	4	48
β-strand	71	1	49
β-strand	76	1	49
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	47
α-helix	113-125	13
β-strand	131-136	6	47
α-helix	137-144	8
β-strand	150-155	6	50
β-strand	160-166	7	50
β-strand	169-170	2	50
α-helix	172-174	3
β-strand	176-178	3	50
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-229	7
α-helix	230-232	3
β-strand	238-241	4	51
β-strand	247-250	4	51
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	50
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	50
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-354	5
β-strand	357-358	2	47
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chains F and G: 9 helices, 10 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
α-helix	26-29	4
β-strand	33-40	8	1
β-strand	46-56	11	1
β-strand	60	1	2
β-strand	64	1	2
α-helix	67-74	8
β-strand	81-91	11	1
β-strand	95-104	10	1
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-137	5	1
α-helix	140-144	5
α-helix	146-153	8
β-strand	158-161	4	1
β-strand	164-165	2	1

Chain H: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	5	1
β-strand	6-7	2	5
α-helix	8	1
α-helix	9-19	11
α-helix	26-29	4
β-strand	33-40	8	5
β-strand	46-56	11	5
β-strand	60	1	6
β-strand	64	1	6
α-helix	67-73	7
β-strand	81-87	7	5
β-strand	89-91	3	7
β-strand	95	1	7
β-strand	98-104	7	5
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-137	5	5
α-helix	140-144	5
α-helix	147-153	7
β-strand	158-161	4	7
β-strand	164-165	2	7

Chain I: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	8
α-helix	9-19	11
α-helix	29-31	3
β-strand	33-40	8	8
β-strand	46-56	11	8
α-helix	67-72	6
β-strand	81-85	5	8
β-strand	88-91	4	9
β-strand	95-97	3	9
β-strand	100-104	5	8
α-helix	111-119	9
α-helix	121-125	5
β-strand	133-137	5	8
α-helix	140-144	5
α-helix	146-153	8
α-helix	155-157	3
β-strand	158-161	4	9
β-strand	164-165	2	9

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	F, G, H, I, J	protein	166	Homo sapiens	P23528 (AlphaFold model)
WD repeat-containing protein 1,Methylated-DNA--protein-cysteine methyltransferase	P	protein	805	Homo sapiens	O75083 (AlphaFold model), P16455 (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

>9QFQ_1 Cofilin-1 (chains F, G, H, I, J)
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDV
GQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS
KDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

Sequence of entity 2 (P), FASTA

>9QFQ_2 WD repeat-containing protein 1,Methylated-DNA--protein-cysteine methyltransferase (chains P)
GAMGSMPYEIKKVFASLPQVERGVSKIIGGDPKGNNFLYTNGKCVILRNIDNPALADIYT
EHAHQVVVAKYAPSGFYIASGDVSGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSK
RIAVVGEGREKFGAVFLWDSGSSVGEITGHNKVINSVDIKQSRPYRLATGSDDNCAAFFE
GPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIYIYDGKTGEKVCALGGSKAHDG
GIYAISWSPDSTHLLSASGDKTSKIWDVSVNSVVSTFPMGSTVLDQQLGCLWQKDHLLSV
SLSGYINYLDRNNPSKPLHVIKGHSKSIQCLTVHKNGGKSYIYSGSHDGHINYWDSETGE
NDSFAGKGHTNQVSRMTVDESGQLISCSMDDTVRYTSLMLRDYSGQGVVKLDVQPKCVAV
GPGGYAVVVCIGQIVLLKDQRKCFSIDNPGYEPEVVAVHPGGDTVAIGGVDGNVRLYSIL
GTTLKDEGKLLEAKGPVTDVAYSHDGAFLAVCDASKVVTVFSVADGYSENNVFYGHHAKI
VCLAWSPDNEHFASGGMDMMVYVWTLSDPETRVKIQDAHRLHHVSSLAWLDEHTLVTTSH
DASVKEWTITYGTGGGGSGGGGSMDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKG
TSAADAVEVPAPAAVLGGPEPLMQATAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQ
VLWKLLKVVKFGEVISYQQLAALAGNPAATAAVKTALSGNPVPILIPCHRVVSSSGAVGG
YEGGLAVKEWLLAHEGHRLGKPGLG

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

>9QFQ_3 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
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	5
MG	Magnesium ion	Mg	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
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)
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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