9Q7L: Barbed end of F-actin and cofilin on sides

Barbed end of F-actin and cofilin on sides. Determined by electron microscopy at 3.68 Å resolution. Released 4 Mar 2026.

Method: Electron microscopy
Resolution: 3.68 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 8
Atoms: 18,286
Mol. weight: 268.45 kDa
Ligands: MG, ADP
Released: 4 Mar 2026

Explore 9Q7L in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q7L contains 134 α-helices and 125 β-strands across 8 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, 9 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	28
α-helix	9-19	11
β-strand	21	1	14
α-helix	26-29	4
β-strand	33-40	8	28
β-strand	46-56	11	28
α-helix	57-59	3
α-helix	67-73	7
β-strand	81-91	11	28
β-strand	94-104	11	28
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-136	4	28
α-helix	140-142	3
α-helix	146-152	7
α-helix	155-157	3
β-strand	158-161	4	28
β-strand	164-165	2	28

Chain A: 19 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	29-32	4	1
β-strand	35-37	3	2
β-strand	53-54	2	2
α-helix	55-60	6
β-strand	66-68	3	2
β-strand	71	1	3
β-strand	76	1	3
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	149-155	7	4
β-strand	160-166	7	4
β-strand	169-170	2	4
β-strand	176-178	3	4
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	252-255	4
α-helix	258-261	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	4
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	370-373	4

Chain b: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	29
α-helix	9-19	11
β-strand	21	1	20
α-helix	26-30	5
β-strand	33-40	8	29
β-strand	46-49	4	29
β-strand	55-56	2	29
α-helix	67-74	8
β-strand	81-91	11	29
β-strand	95-104	10	29
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-136	4	29
α-helix	140-142	3
α-helix	146-152	7
α-helix	155-157	3
β-strand	158-161	4	29
β-strand	165	1	29

Chain B: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	6
β-strand	16-21	6	6
β-strand	29-32	4	6
β-strand	35-38	4	7
β-strand	53-54	2	7
α-helix	55-60	6
β-strand	65-68	4	7
β-strand	71	1	8
β-strand	76	1	8
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	6
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	6
α-helix	137-144	8
β-strand	149-155	7	9
β-strand	160-166	7	9
β-strand	170	1	9
β-strand	176-178	3	9
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	252-254	3
α-helix	258-261	4
α-helix	264-266	3
α-helix	274-283	10
α-helix	287-289	3
α-helix	291-294	4
β-strand	297-300	4	9
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain c: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	5	1
β-strand	6	1	30
α-helix	7-8	2
α-helix	9-19	11
β-strand	33-40	8	31
β-strand	46	1	30
β-strand	47-56	10	31
α-helix	57-59	3
α-helix	67-74	8
β-strand	81-91	11	31
β-strand	94-104	11	31
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-136	4	31
α-helix	146-152	7
β-strand	158-161	4	31
β-strand	164-165	2	31

Chain C: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	11
β-strand	16-21	6	11
β-strand	29-32	4	11
β-strand	35-38	4	12
β-strand	53-54	2	12
α-helix	55-57	3
β-strand	65-68	4	12
β-strand	71	1	13
β-strand	76	1	13
α-helix	79-88	10
α-helix	89-93	5
β-strand	96	1	14
α-helix	98-100	3
β-strand	103-107	5	11
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	11
α-helix	137-144	8
β-strand	149-155	7	15
β-strand	160-166	7	15
β-strand	169-170	2	15
β-strand	176-178	3	15
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	16
β-strand	247-250	4	16
α-helix	252-254	3
α-helix	259-261	3
α-helix	264-266	3
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	15
α-helix	309-320	12
β-strand	329-330	2	15
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain D: 22 helices, 20 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	55-57	3
β-strand	65-68	4	18
β-strand	71	1	19
β-strand	76	1	19
α-helix	79-88	10
α-helix	89-93	5
β-strand	96	1	20
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	21
β-strand	160-166	7	21
β-strand	169-170	2	21
β-strand	176-178	3	21
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	22
β-strand	247-250	4	22
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-266	3
α-helix	274-283	10
α-helix	287-289	3
α-helix	291-294	4
β-strand	297-300	4	21
α-helix	309-320	12
β-strand	329-330	2	21
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	17
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain E: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	23
β-strand	16-21	6	23
β-strand	29-32	4	23
β-strand	35-38	4	24
β-strand	53-54	2	24
α-helix	56-59	4
β-strand	65-68	4	24
β-strand	71	1	25
β-strand	76	1	25
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	23
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	23
α-helix	137-144	8
β-strand	150-155	6	26
β-strand	160-166	7	26
β-strand	169-170	2	26
β-strand	176-178	3	26
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	27
β-strand	247-250	4	27
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-266	3
α-helix	274-283	10
α-helix	287-289	3
α-helix	291-294	4
β-strand	297-300	4	26
α-helix	303-305	3
α-helix	309-320	12
α-helix	325-327	3
β-strand	329-330	2	26
α-helix	338-347	10
α-helix	353-355	3
β-strand	357-358	2	23
α-helix	359-364	6
α-helix	367-369	3
α-helix	370-373	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D, E	protein	376	Oryctolagus cuniculus	P68135 (AlphaFold model)
Cofilin-2	a, b, c	protein	166	Homo sapiens	Q9Y281 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>9Q7L_1 Actin, alpha skeletal muscle (chains A, B, C, D, E)
CDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK
QEYDEAGPSIVHRKCF

Sequence of entity 2 (a, b, c), FASTA

>9Q7L_2 Cofilin-2 (chains a, b, c)
MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDI
GDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS
KDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL

Ligands and cofactors

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

Primary citation

Mechanisms of disassembly at the actin filament pointed and barbed ends. Palmer, N.J., Boczkowska, M., Rebowski, G. et al. Sci Adv (2026) 12:eaee5882-eaee5882. DOI 10.1126/sciadv.aee5882 · PubMed

Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4B1Y 1.29 Å, Structure of the Phactr1 RPEL-3 bound to G-actin
2FXU 1.35 Å, X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
4K41 1.4 Å, Crystal structure of actin in complex with marine macrolide kabiramide C
1QZ5 1.45 Å, Structure of rabbit actin in complex with kabiramide C
1WUA 1.45 Å, The structure of Aplyronine A-actin complex
2Q0U 1.45 Å, Structure of Pectenotoxin-2 and Latrunculin B Bound to Actin
2V52 1.45 Å, Structure of MAL-RPEL2 complexed to G-actin
3MN5 1.5 Å, Structures of actin-bound WH2 domains of Spire and the implication for filament nucleation
2PBD 1.5 Å, Ternary complex of profilin-actin with the poly-PRO-GAB domain of VASP*
5ZZA 1.53 Å, OdinProfilin/Rabbit Actin Complex
1J6Z 1.54 Å, Uncomplexed actin
1QZ6 1.6 Å, Structure of rabbit actin in complex with jaspisamide A

Browse structure collections

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