9AZQ: Actin, alpha skeletal muscle

INF2 at the Barbed End of F-Actin with Incoming Actin. Determined by electron microscopy at 3.82 Å resolution. Released 29 May 2024.

Method: Electron microscopy
Resolution: 3.82 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 9
Atoms: 23,563
Mol. weight: 336.6 kDa
Ligands: MG, ADP
Released: 29 May 2024

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

Secondary structure: helices and β-sheets

9AZQ contains 182 α-helices and 141 β-strands across 9 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: 23 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	35-38	4	2
β-strand	53-54	2	2
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	2
β-strand	71-72	2	3
β-strand	75-76	2	3
α-helix	79-88	10
α-helix	89-93	5
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	4
β-strand	160-166	7	4
β-strand	169-170	2	4
β-strand	176-178	3	4
α-helix	182-192	11
α-helix	193-195	3
α-helix	203-215	13
α-helix	223-232	10
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	4
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

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	35-38	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	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	6
α-helix	113-125	13
β-strand	131-136	6	6
α-helix	137-145	9
β-strand	150-155	6	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	182-192	11
α-helix	193-195	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	253-256	4
α-helix	259-262	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	303-305	3
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	369-373	5

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	79-88	10
α-helix	89-93	5
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	137-145	9
β-strand	150-155	6	14
β-strand	160-166	7	14
β-strand	169-170	2	14
β-strand	176-178	3	14
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	15
β-strand	247-250	4	15
α-helix	253-262	10
α-helix	264-266	3
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	14
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	369-373	5

Chain D: 22 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	42	1	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	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-123	11
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	203-215	13
α-helix	223-232	10
β-strand	238-241	4	20
β-strand	247-250	4	20
α-helix	253-256	4
α-helix	259-262	4
α-helix	274-284	11
α-helix	290-295	6
β-strand	297-300	4	19
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	338-348	11
α-helix	351-355	5
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	366-368	3
α-helix	370-373	4

Chain E: 24 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	42	1	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	1	23
β-strand	76	1	23
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	21
α-helix	113-121	9
α-helix	122-126	5
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	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	259-262	4
α-helix	264-266	3
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	24
α-helix	303-305	3
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	366-368	3
α-helix	369-373	5

Chain F: 21 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	26
β-strand	16-21	6	26
β-strand	29-32	4	26
β-strand	35-38	4	27
β-strand	41-42	2	19
β-strand	53-54	2	27
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	27
β-strand	71-72	2	28
β-strand	75-76	2	28
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	26
α-helix	113-125	13
β-strand	131-136	6	26
α-helix	137-145	9
β-strand	150-155	6	29
β-strand	160-166	7	29
β-strand	169-170	2	29
β-strand	176-178	3	29
α-helix	182-192	11
α-helix	203-215	13
α-helix	223-232	10
β-strand	238-241	4	30
β-strand	247-250	4	30
α-helix	253-262	10
α-helix	264-266	3
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	29
α-helix	309-320	12
β-strand	329-330	2	29
α-helix	335-337	3
α-helix	338-345	8
α-helix	350-352	3
β-strand	357-358	2	26
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain G: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	558-560	3
β-strand	564	1	31
α-helix	565-567	3
α-helix	570-573	4
α-helix	574-577	4
α-helix	584-587	4
α-helix	599-605	7
β-strand	607	1	31
α-helix	608-609	2

Chain H: 15 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	635-646	12
α-helix	652-661	10
α-helix	669-677	9
α-helix	682-689	8
α-helix	695-697	3
α-helix	700-710	11
α-helix	714-749	36
α-helix	754-768	15
α-helix	782-784	3
β-strand	792	1	32
β-strand	799	1	32
α-helix	800-810	11
α-helix	813-817	5
α-helix	818-821	4
α-helix	833-855	23
α-helix	859-896	38
α-helix	907-946	40

1 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, F, I	protein	371	Oryctolagus cuniculus	P68135 (AlphaFold model)
Inverted formin-2	G	protein	60	Homo sapiens	Q27J81 (AlphaFold model)
Inverted formin-2	H	protein	323	Homo sapiens	Q27J81 (AlphaFold model)

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

>9AZQ_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F, I)
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGI
LTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMF
ETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRD
LTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPD
GQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDE
AGPSIVHRKCF

Sequence of entity 2 (G), FASTA

>9AZQ_2 Inverted formin-2 (chains G)
VPSHRRVNPPTLRMKKLNWQKLPSNVAREHNSMWASLSSPDAEAVEPDFSSIERLFSFPA

Sequence of entity 3 (H), FASTA

>9AZQ_3 Inverted formin-2 (chains H)
KEPKEITFLDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHE
IENLRAFTEERAKLASADHFYLLLLAIPCYQLRIECMLLCEGAAAVLDMVRPKAQLVLAA
CESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTETKSQQNRVTLLHHV
LEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEASSNLKKLLETERKVSASVAEVQEQ
YTERLQASISAFRALDELFEAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLFLRAL
KENKDRKEQAAKAERRKQQLAEE

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	7
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	7

Primary citation

Mechanisms of actin filament severing and elongation by formins. Palmer, N.J., Barrie, K.R., Dominguez, R. Nature (2024) 632:437-442. DOI 10.1038/s41586-024-07637-0 · 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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