9DFS: Actin, alpha skeletal muscle

Structure of novel Myo7a-N isoform (ADP-bound) expressed in sensory hair cells (head domain + first two IQ domains), bound to F-actin. Determined by electron microscopy at 3.1 Å resolution. Released 10 Sept 2025.

Method: Electron microscopy
Resolution: 3.1 Å
Organisms: Oryctolagus cuniculus, Mus musculus
Chains: 4
Atoms: 14,306
Mol. weight: 250.94 kDa
Ligands: MG, ADP
Released: 10 Sept 2025

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

Secondary structure: helices and β-sheets

9DFS contains 98 α-helices and 88 β-strands across 4 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, 20 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	35-38	4	2
β-strand	41-42	2	3
β-strand	53-54	2	2
α-helix	55-57	3
β-strand	65-68	4	2
β-strand	71-72	2	4
β-strand	75-76	2	4
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	131-136	6	1
α-helix	137-145	9
β-strand	150-155	6	5
β-strand	160-166	7	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	176-178	3	5
α-helix	182-192	11
α-helix	206-216	11
α-helix	223-232	10
β-strand	238-241	4	6
β-strand	247-250	4	6
α-helix	253-256	4
α-helix	257-259	3
α-helix	264-266	3
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	5
α-helix	309-318	10
β-strand	329-330	2	5
α-helix	335-337	3
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain B: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	7
β-strand	16-21	6	7
β-strand	24	1	8
β-strand	29-32	4	7
β-strand	35-38	4	9
α-helix	48-49	2
β-strand	53-54	2	9
α-helix	56-60	5
β-strand	65-68	4	9
β-strand	71-72	2	10
β-strand	75-76	2	10
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	7
α-helix	113-125	13
β-strand	131-136	6	7
α-helix	137-145	9
β-strand	150-155	6	3
β-strand	160-166	7	3
β-strand	169-170	2	3
α-helix	172-174	3
β-strand	176-178	3	3
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	11
β-strand	247-250	4	11
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	3
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	3
α-helix	338-348	11
α-helix	351-355	5
β-strand	357-358	2	7
α-helix	359-365	7
α-helix	369-373	5

Chain C: 22 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	12
β-strand	11-12	2	13
β-strand	16-18	3	13
β-strand	21	1	12
β-strand	31-32	2	13
β-strand	35-36	2	14
β-strand	37-38	2	15
β-strand	53-54	2	14
α-helix	57-60	4
β-strand	65-66	2	15
β-strand	71-72	2	16
β-strand	75-76	2	16
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	12
α-helix	113-125	13
β-strand	131-136	6	12
α-helix	137-145	9
β-strand	150-155	6	17
β-strand	160-166	7	17
β-strand	169-170	2	17
α-helix	172-174	3
β-strand	176-178	3	17
α-helix	182-192	11
α-helix	193-195	3
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	18
β-strand	247-250	4	18
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-282	9
α-helix	289-294	6
β-strand	297-300	4	17
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	17
α-helix	338-347	10
β-strand	357-358	2	12
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain D: 30 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	41-44	4	19
β-strand	56-61	6	19
β-strand	69-72	4	19
β-strand	77-79	3	19
β-strand	90	1	19
α-helix	91-92	2
α-helix	93-97	5
β-strand	101	1	20
α-helix	102-104	3
α-helix	110-121	12
β-strand	127-130	4	20
β-strand	133-137	5	20
α-helix	148-153	6
β-strand	159	1	21
β-strand	162	1	21
α-helix	166-180	15
β-strand	184-190	7	20
α-helix	196-211	16
α-helix	215-231	17
β-strand	233-234	2	22
β-strand	242-243	2	22
β-strand	246-253	8	20
β-strand	259-267	9	20
α-helix	271-274	4
α-helix	285-292	8
α-helix	298-301	4
α-helix	328-339	12
α-helix	344-360	17
β-strand	365-369	5	23
β-strand	374-378	5	23
α-helix	379-380	2
α-helix	382-391	10
α-helix	395-402	8
β-strand	404-409	6	24
β-strand	412-417	6	24
α-helix	420-450	31
β-strand	464-470	7	20
β-strand	479	1	25
α-helix	481-511	31
α-helix	525-531	7
α-helix	538-547	10
α-helix	553-564	12
β-strand	570-571	2	25
β-strand	580-584	5	25
β-strand	589-593	5	25
α-helix	607-614	8
α-helix	619-624	6
α-helix	626-630	5
α-helix	632-634	3
β-strand	637	1	8
α-helix	638-641	4
α-helix	642-658	17
β-strand	661-668	8	20
α-helix	681-690	10
α-helix	694-702	9
α-helix	710-714	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Unconventional myosin-VIIa	D	protein	1077	Mus musculus	P97479 (AlphaFold model)

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

>9DFS_1 Actin, alpha skeletal muscle (chains A, B, C)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (D), FASTA

>9DFS_2 Unconventional myosin-VIIa (chains D)
GNKAGMESPGSPADPGEAPAPPPGKWALVRNLNQTLKTFAVLPGDYVWMDLKSGQEFDVP
IGAVVKLCDSGQIQVVDDEDNEHWISPQNATHIKPMHPTSVHGVEDMIRLGDLNEAGILR
NLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYTNKKIGEMPPHIFAIADNCYF
NMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHSWIEQQVLEATPILEAFGNAK
TIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVCRQAPDERNYHVFYCMLEGMN
EEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRSAMKVLMFTDTENWEISKLLA
AILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNPPDLMSCLTSRTLITRGETVS
TPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPPLEVKNSRRSIGLLDIFGFEN
FTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESIDWLHIEFTDNQEALDMIANRP
MNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKNSHETQFGINHFAGVVYYESQ
GFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAETRKRSPTLSSQFKRSLELLMR
TLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMMETIRIRHAGYPIRYSFVEFVE
RYRVLLPGVKPAYKQGDLRGTCQRMAEAVLGTHDDWQIGKTKIFLKDHHDMLLEVERDKA
ITDRVILLQKVIRGFKDRSNFLRLKSAATLIQRHWRGHHCRKNYEGSMVSKGEELFTGVV
PILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFS
RYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKE
DGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGP
VLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMDELYKAAADYKDDDDK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	4
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	4

Primary citation

Tonotopic specialization of MYO7A isoforms in auditory hair cells. Li, S., Park, J., Phan, T.M. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-73220-y · 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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