9Y52: One CAP-1

One CAP-1 Bound to the Pointed End of Cofilin F-actin. Determined by electron microscopy at 3.46 Å resolution. Released 4 Mar 2026.

Method: Electron microscopy
Resolution: 3.46 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 11
Atoms: 22,387
Mol. weight: 357.95 kDa
Ligands: MG, ADP
Released: 4 Mar 2026

Explore 9Y52 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Y52 contains 169 α-helices and 142 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: 9 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	30
α-helix	9-19	11
β-strand	21	1	14
α-helix	26-30	5
β-strand	33-40	8	30
β-strand	46-56	11	30
α-helix	57-59	3
α-helix	67-73	7
β-strand	81-91	11	30
β-strand	95-104	10	30
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-136	4	30
α-helix	140-142	3
α-helix	146-152	7
α-helix	155-157	3
β-strand	158-161	4	30
β-strand	164-165	2	30

Chain A: 25 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
α-helix	38-40	3
β-strand	53-54	2	2
α-helix	55-57	3
β-strand	66-68	3	2
β-strand	71	1	3
β-strand	76	1	3
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	131-136	6	1
α-helix	137-145	9
β-strand	149-155	7	4
β-strand	160-166	7	4
β-strand	169-170	2	4
α-helix	172-174	3
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	252-254	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	4
α-helix	303-305	3
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	4
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chains b and c: 9 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	31
α-helix	9-19	11
β-strand	21	1	21
α-helix	26-30	5
β-strand	33-40	8	31
β-strand	46-56	11	31
α-helix	57-59	3
α-helix	67-72	6
β-strand	81-91	11	31
β-strand	95-104	10	31
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-136	4	31
α-helix	140-142	3
α-helix	147-152	6
α-helix	155-157	3
β-strand	158-161	4	31
β-strand	164-165	2	31

Chain B: 24 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	35-37	3	7
β-strand	53-54	2	7
α-helix	58-60	3
β-strand	66-68	3	7
β-strand	71	1	8
β-strand	76	1	8
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	6
α-helix	113-125	13
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	169-170	2	9
α-helix	172-174	3
β-strand	176-178	3	9
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	10
β-strand	247-250	4	10
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	290-294	5
β-strand	297-300	4	9
α-helix	302-304	3
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	9
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain C: 22 helices, 21 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	58-60	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	113-125	13
β-strand	131-132	2	15
β-strand	134-136	3	11
α-helix	137-143	7
β-strand	149-155	7	16
β-strand	160-166	7	16
β-strand	169-170	2	16
β-strand	176-178	3	16
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	17
β-strand	247-250	4	17
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	290-294	5
β-strand	297-300	4	16
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	16
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	15
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain d: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	33
α-helix	9-19	11
α-helix	21-23	3
α-helix	26-30	5
β-strand	33-40	8	33
β-strand	46-56	11	33
α-helix	57-59	3
α-helix	67-73	7
β-strand	81-91	11	33
β-strand	95-104	10	33
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-136	4	33
α-helix	140-142	3
α-helix	147-152	6
α-helix	155-157	3
β-strand	158-161	4	33
β-strand	164-165	2	33

Chain D: 20 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	18
β-strand	16-21	6	18
β-strand	29-32	4	18
β-strand	35-38	4	19
β-strand	53-54	2	19
α-helix	58-60	3
β-strand	65-68	4	19
β-strand	71	1	20
β-strand	76	1	20
α-helix	79-88	10
α-helix	89-93	5
β-strand	96	1	21
β-strand	103-107	5	18
α-helix	113-125	13
β-strand	131-136	6	18
α-helix	137-144	8
β-strand	149-155	7	22
β-strand	160-166	7	22
β-strand	169-170	2	22
β-strand	176-178	3	22
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	23
β-strand	247-250	4	23
α-helix	252-254	3
α-helix	258-261	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-293	4
β-strand	297-300	4	22
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	22
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	18
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain e: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	34
α-helix	9-19	11
α-helix	26-30	5
β-strand	33-40	8	34
β-strand	46-56	11	34
α-helix	57-59	3
α-helix	67-73	7
β-strand	81-91	11	34
β-strand	95-104	10	34
α-helix	111-119	9
α-helix	121-127	7
β-strand	133-136	4	34
α-helix	140-142	3
α-helix	147-152	6
α-helix	155-157	3
β-strand	158-161	4	34
β-strand	164-165	2	34

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
Actin, alpha skeletal muscle	A, B, C, D, E	protein	376	Oryctolagus cuniculus	P68135 (AlphaFold model)
Adenylyl cyclase-associated protein 1	W	protein	475	Homo sapiens	Q01518 (AlphaFold model)
Cofilin-2	a, b, c, d, e	protein	166	Homo sapiens	Q9Y281 (AlphaFold model)

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

>9Y52_1 Actin, alpha skeletal muscle (chains A, B, C, D, E)
CDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK
QEYDEAGPSIVHRKCF

Sequence of entity 2 (W), FASTA

>9Y52_2 Adenylyl cyclase-associated protein 1 (chains W)
MADMQNLVERLERAVGRLEAVSHTSDMHRGYADSPSKAGAAPYVQAFDSLLAGPVAEYLK
ISKEIGGDVQKHAEMVHTGLKLERALLVTASQCQQPAENKLSDLLAPISEQIKEVITFRE
KNRGSKLFNHLSAVSESIQALGWVAMAPKPGPYVKEMNDAAMFYTNRVLKEYKDVDKKHV
DWVKAYLSIWTELQAYIKEFHTTGLAWSKTGPVAKELSGLPSGPSAGSCPPPPPPCPPPP
PVSTISCSYESASRSSLFAQINQGESITHALKHVSDDMKTHKNPALKAQSGPVRSGPKPF
SAPKPQTSPSPKRATKKEPAVLELEGKKWRVENQENVSNLVIEDTELKQVAYIYKCVNTT
LQIKGKINSITVDNCKKLGLVFDDVVGIVEIINSKDVKVQVMGKVPTISINKTDGCHAYL
SKNSLDCEIVSAKSSEMNVLIPTEGGDFNEFPVPEQFKTLWNGQKLVTTVTEIAG

Sequence of entity 3 (a, b, c, d, e), FASTA

>9Y52_3 Cofilin-2 (chains a, b, c, d, e)
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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