9DFV: Actin, alpha skeletal muscle

Structure of canonical Myo7a-C 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: 14,247
Mol. weight: 204.92 kDa
Ligands: ADP, MG
Released: 10 Sept 2025

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

Secondary structure: helices and β-sheets

9DFV contains 107 α-helices and 83 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: 26 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	57-60	4
α-helix	62-64	3
β-strand	65-68	4	2
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	81-87	7
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	149-155	7	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	193-195	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	6
β-strand	247-250	4	6
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	289-295	7
β-strand	297-300	4	5
α-helix	302-305	4
α-helix	309-320	12
α-helix	326-327	2
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	369-373	5

Chain B: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	7
β-strand	16-21	6	7
β-strand	29-32	4	7
β-strand	35-38	4	8
β-strand	53-54	2	8
α-helix	56-60	5
β-strand	65-68	4	8
β-strand	71-72	2	9
β-strand	75-76	2	9
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	7
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	7
α-helix	137-145	9
β-strand	149-155	7	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	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-295	6
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	351-354	4
β-strand	357-358	2	7
α-helix	359-365	7
α-helix	369-373	5

Chain C: 26 helices, 19 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	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	81-87	7
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	193-195	3
α-helix	206-216	11
α-helix	223-230	8
β-strand	238-241	4	15
β-strand	247-250	4	15
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	14
α-helix	302-305	4
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	14
α-helix	335-337	3
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain D: 32 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	9-12	4	16
β-strand	26-27	2	16
α-helix	53-55	3
β-strand	56-58	3	16
α-helix	59-60	2
α-helix	61-64	4
β-strand	69	1	17
α-helix	70-72	3
α-helix	78-90	13
β-strand	95-97	3	17
β-strand	101-105	5	17
α-helix	116-122	7
β-strand	127	1	18
β-strand	130	1	18
α-helix	134-148	15
β-strand	152-158	7	17
α-helix	164-178	15
α-helix	184-200	17
β-strand	201-202	2	19
β-strand	210-211	2	19
β-strand	214-220	7	17
β-strand	229-235	7	17
α-helix	240-242	3
β-strand	252	1	19
α-helix	253-259	7
α-helix	264-270	7
α-helix	279-282	4
α-helix	289	1
α-helix	294-307	14
α-helix	312-329	18
β-strand	333-336	4	20
β-strand	343-346	4	20
α-helix	347-348	2
α-helix	350-359	10
α-helix	363-371	9
β-strand	372-374	3	21
β-strand	383-385	3	21
α-helix	388-418	31
β-strand	433-439	7	17
β-strand	447	1	22
α-helix	449-472	24
α-helix	477-481	5
α-helix	494-496	3
α-helix	497-501	5
α-helix	506-515	10
α-helix	521-532	12
β-strand	538-539	2	22
β-strand	548-552	5	22
β-strand	557-561	5	22
β-strand	563-566	4	23
α-helix	575-583	9
α-helix	587-592	6
α-helix	603-605	3
α-helix	610-627	18
β-strand	629-636	8	17
α-helix	649-659	11
α-helix	662-670	9

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	670	Mus musculus	P97479 (AlphaFold model)

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

>9DFV_1 Actin, alpha skeletal muscle (chains A, B, C)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (D), FASTA

>9DFV_2 Unconventional myosin-VIIa (chains D)
LQKGDYVWMDLKSGQEFDVPIGAVVKLCDSGQIQAVDDEDNEHWISPQNATHIKPMHPTS
VHGVEDMIRLGDLNEAGILRNLLIRYRDHLIYTYTGSILVAVNPYQLLSIYSPEHIRQYT
NKKIGEMPPHIFAIADNCYFNMKRNNRDQCCIISGESGAGKTESTKLILQFLAAISGQHS
WIEQQVLEATPILEAFGNAKTIRNDNSSRFGKYIDIHFNKRGAIEGAKIEQYLLEKSRVC
RQAPDERNYHVFYCMLEGMNEEEKKKLGLGQAADYNYLAMGNCITCEGRVDSQEYANIRS
AMKVLMFTDTENWEISKLLAAILHMGNLQYEARTFENLDACEVLFSPSLATAASLLEVNP
PDLMSCLTSRTLITRGETVSTPLSREQALDVRDAFVKGIYGRLFVWIVEKINAAIYKPPP
LEVKNSRRSIGLLDIFGFENFTVNSFEQLCINFANEHLQQFFVRHVFKLEQEEYDLESID
WLHIEFTDNQEALDMIANRPMNVISLIDEESKFPKGTDATMLHKLNSQHKLNANYVPPKN
SHETQFGINHFAGVVYYESQGFLEKNRDTLHGDIIQLVHSSRNKFIKQIFQADVAMGAET
RKRSPTLSSQFKRSLELLMRTLGACQPFFVRCIKPNEFKKPMLFDRHLCVRQLRYSGMME
TIRIRHAGYP

Ligands and cofactors

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