9Q7O: One CAP-1

One CAP-1 Bound to the Pointed End of F-actin. Determined by electron microscopy at 3.02 Å resolution. Released 4 Mar 2026.

Method: Electron microscopy
Resolution: 3.02 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 6
Atoms: 15,919
Mol. weight: 264.12 kDa
Ligands: ADP, MG
Released: 4 Mar 2026

Explore 9Q7O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q7O contains 119 α-helices and 97 β-strands across 6 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: 22 helices, 18 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	1	2
α-helix	56-60	5
β-strand	66-68	3	2
β-strand	71-72	2	3
β-strand	75-76	2	3
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	132-136	5	1
α-helix	137-143	7
β-strand	150-155	6	4
β-strand	160-165	6	4
β-strand	169-170	2	4
β-strand	176-178	3	4
α-helix	182-195	14
α-helix	203-205	3
α-helix	206-214	9
α-helix	223-231	9
β-strand	238-242	5	5
β-strand	246-250	5	5
α-helix	254-256	3
α-helix	259-261	3
α-helix	264-266	3
α-helix	274-283	10
α-helix	290-293	4
β-strand	297-300	4	4
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-347	10
α-helix	351-354	4
α-helix	359-365	7
α-helix	366-368	3
α-helix	370-373	4

Chain B: 21 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	56-60	5
α-helix	62-64	3
β-strand	65-68	4	7
β-strand	71-72	2	8
β-strand	75-76	2	8
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-105	3	6
α-helix	113-125	13
β-strand	131-134	4	6
α-helix	137-143	7
β-strand	150-155	6	9
β-strand	160-165	6	9
β-strand	169-170	2	9
β-strand	176-178	3	9
α-helix	182-194	13
α-helix	206-214	9
α-helix	223-231	9
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	252-254	3
α-helix	259-261	3
α-helix	274-284	11
α-helix	290-293	4
β-strand	297-300	4	9
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	366-368	3
α-helix	370-373	4

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	41-42	2	4
β-strand	53-54	2	12
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	12
β-strand	71-72	2	13
β-strand	75-76	2	13
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	11
α-helix	113-125	13
β-strand	131-136	6	11
α-helix	137-145	9
β-strand	150-155	6	14
β-strand	160-166	7	14
β-strand	169-170	2	14
α-helix	172-174	3
β-strand	176-178	3	14
α-helix	182-192	11
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	15
β-strand	247-250	4	15
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
β-strand	297-300	4	14
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	366-368	3
α-helix	370-373	4

Chain D: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	16
β-strand	16-21	6	16
β-strand	29-32	4	16
β-strand	35-38	4	17
β-strand	41-42	2	9
β-strand	53-54	2	17
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	17
β-strand	71-72	2	18
β-strand	75-76	2	18
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-125	13
β-strand	131-136	6	16
α-helix	137-145	9
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	182-192	11
α-helix	193-195	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	20
β-strand	247-250	4	20
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
β-strand	297-300	4	19
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain E: 22 helices, 20 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	41-42	2	14
β-strand	53-54	2	22
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	22
β-strand	71-72	2	23
β-strand	75-76	2	23
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	21
α-helix	113-125	13
β-strand	131-136	6	21
α-helix	137-145	9
β-strand	150-155	6	24
β-strand	160-166	7	24
β-strand	169-170	2	24
α-helix	172-174	3
β-strand	176-178	3	24
α-helix	182-192	11
α-helix	193-195	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	25
β-strand	247-250	4	25
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
β-strand	297-300	4	24
α-helix	309-320	12
β-strand	329-330	2	24
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	21
α-helix	359-365	7
α-helix	369-373	5

Chain W: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	56-64	9
α-helix	65-69	5
α-helix	70-79	10
α-helix	82-106	25
α-helix	112-135	24
α-helix	142-149	8
α-helix	152-157	6
α-helix	164-186	23
α-helix	191-214	24

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)

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

>9Q7O_1 Actin, alpha skeletal muscle (chains A, B, C, D, E)
CDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK
QEYDEAGPSIVHRKCF

Sequence of entity 2 (W), FASTA

>9Q7O_2 Adenylyl cyclase-associated protein 1 (chains W)
MADMQNLVERLERAVGRLEAVSHTSDMHRGYADSPSKAGAAPYVQAFDSLLAGPVAEYLK
ISKEIGGDVQKHAEMVHTGLKLERALLVTASQCQQPAENKLSDLLAPISEQIKEVITFRE
KNRGSKLFNHLSAVSESIQALGWVAMAPKPGPYVKEMNDAAMFYTNRVLKEYKDVDKKHV
DWVKAYLSIWTELQAYIKEFHTTGLAWSKTGPVAKELSGLPSGPSAGSCPPPPPPCPPPP
PVSTISCSYESASRSSLFAQINQGESITHALKHVSDDMKTHKNPALKAQSGPVRSGPKPF
SAPKPQTSPSPKRATKKEPAVLELEGKKWRVENQENVSNLVIEDTELKQVAYIYKCVNTT
LQIKGKINSITVDNCKKLGLVFDDVVGIVEIINSKDVKVQVMGKVPTISINKTDGCHAYL
SKNSLDCEIVSAKSSEMNVLIPTEGGDFNEFPVPEQFKTLWNGQKLVTTVTEIAG

Ligands and cofactors

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