7U8K: Actin, alpha skeletal muscle

Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments. Determined by solid-state NMR. Released 16 Aug 2023.

Method: Solid-state NMR
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 18
Atoms: 39,920
Mol. weight: 569.18 kDa
Released: 16 Aug 2023

Explore 7U8K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7U8K contains 292 α-helices and 262 β-strands across 18 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: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	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	56-59	4
β-strand	65-68	4	2
α-helix	82-88	7
α-helix	89-94	6
β-strand	96	1	3
β-strand	103-107	5	1
α-helix	115-124	10
β-strand	131-136	6	1
α-helix	138-144	7
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	184-194	11
α-helix	203-216	14
α-helix	223-231	9
α-helix	234-236	3
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	4
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-346	9
α-helix	350-354	5
β-strand	357-358	2	1
α-helix	361-364	4
α-helix	367-369	3
α-helix	370-373	4

Chain B: 20 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	6
β-strand	16-21	6	6
β-strand	22	1	7
β-strand	24	1	7
β-strand	29-32	4	6
β-strand	35-38	4	8
β-strand	53-54	2	8
α-helix	56-59	4
β-strand	65-68	4	8
α-helix	82-88	7
α-helix	89-94	6
β-strand	103-107	5	6
α-helix	113-125	13
β-strand	131-136	6	6
α-helix	137-144	8
β-strand	150-155	6	9
β-strand	160-166	7	9
β-strand	169-170	2	9
β-strand	176-178	3	9
α-helix	182-194	13
α-helix	203-215	13
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	264-267	4
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
β-strand	329-330	2	9
α-helix	338-346	9
α-helix	350-354	5
β-strand	357-358	2	6
α-helix	360-363	4
α-helix	366-371	6

Chain C: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	11
β-strand	16-21	6	11
β-strand	22	1	12
β-strand	24	1	12
β-strand	29-32	4	11
β-strand	35-38	4	13
α-helix	39	1
β-strand	53-54	2	13
α-helix	57-60	4
β-strand	65-68	4	13
β-strand	71-72	2	14
β-strand	75-76	2	14
α-helix	82-88	7
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	11
α-helix	108	1
α-helix	114-124	11
β-strand	131	1	15
β-strand	132-136	5	11
α-helix	137-145	9
β-strand	150-155	6	16
β-strand	160-166	7	16
β-strand	169-170	2	16
α-helix	172-174	3
β-strand	176-178	3	16
α-helix	182-195	14
α-helix	203-216	14
α-helix	219-220	2
α-helix	223-230	8
α-helix	234-236	3
β-strand	238-241	4	17
β-strand	247-250	4	17
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-266	3
α-helix	271-273	3
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	16
α-helix	302-305	4
α-helix	309-318	10
β-strand	329-330	2	16
α-helix	338-347	10
β-strand	358	1	15
α-helix	362-365	4
α-helix	366-372	7

Chain D: 20 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	18
β-strand	16-21	6	18
β-strand	29-32	4	18
β-strand	35-38	4	19
α-helix	42-45	4
β-strand	53-54	2	19
α-helix	56-59	4
β-strand	65-68	4	19
β-strand	71	1	20
β-strand	76	1	20
α-helix	79-88	10
α-helix	89-94	6
β-strand	103-107	5	18
α-helix	115-125	11
β-strand	131-136	6	18
α-helix	137-145	9
β-strand	150-155	6	21
β-strand	160-166	7	21
β-strand	169-170	2	21
α-helix	172-174	3
β-strand	176-178	3	21
α-helix	185-194	10
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	22
β-strand	247-250	4	22
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-282	9
α-helix	290-293	4
β-strand	297-299	3	21
α-helix	309-320	12
β-strand	329-330	2	21
α-helix	338-346	9
α-helix	353-355	3
β-strand	357-358	2	18
α-helix	359-365	7
α-helix	367-372	6

Chain E: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	23
β-strand	16-21	6	23
β-strand	29-32	4	23
β-strand	35-38	4	24
α-helix	39	1
β-strand	53-54	2	24
α-helix	56-59	4
β-strand	65-68	4	24
β-strand	71	1	25
β-strand	76	1	25
α-helix	82-88	7
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	23
α-helix	108	1
α-helix	114-125	12
β-strand	131-136	6	23
α-helix	137-144	8
β-strand	150-155	6	26
β-strand	160-166	7	26
β-strand	169-170	2	26
α-helix	172-174	3
β-strand	176-178	3	26
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-232	10
α-helix	234-236	3
β-strand	238-241	4	27
β-strand	247-250	4	27
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-266	3
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-298	2	26
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	26
α-helix	338-346	9
β-strand	357-358	2	23
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain F: 20 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	28
β-strand	16-21	6	28
β-strand	29-32	4	28
β-strand	35-38	4	29
β-strand	53-54	2	29
α-helix	56-59	4
β-strand	65-68	4	29
α-helix	82-88	7
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	28
α-helix	108	1
α-helix	114-125	12
β-strand	131	1	30
β-strand	132-136	5	28
α-helix	137-145	9
β-strand	150-155	6	31
β-strand	160-166	7	31
β-strand	169-170	2	31
β-strand	176-178	3	31
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-215	13
α-helix	223-231	9
β-strand	238-241	4	32
β-strand	247-250	4	32
α-helix	253-259	7
α-helix	271-273	3
α-helix	274-283	10
α-helix	290-293	4
β-strand	297-299	3	31
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	31
α-helix	338-347	10
β-strand	350	1	33
β-strand	358	1	30
α-helix	362-365	4
α-helix	367-371	5

Chain G: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
α-helix	6-7	2
β-strand	8-12	5	34
β-strand	17-21	5	34
β-strand	22	1	35
β-strand	24	1	35
β-strand	29-31	3	34
β-strand	35-37	3	36
α-helix	46-48	3
β-strand	53-54	2	36
α-helix	57-60	4
α-helix	65	1
β-strand	66-68	3	36
α-helix	82-88	7
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	34
α-helix	113-125	13
β-strand	131-136	6	34
α-helix	137-144	8
β-strand	150-155	6	37
β-strand	160-166	7	37
β-strand	169-170	2	37
α-helix	172-174	3
β-strand	176-178	3	37
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	38
β-strand	247-250	4	38
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-282	9
α-helix	287-294	8
β-strand	297-300	4	37
α-helix	303-305	3
α-helix	309-318	10
β-strand	329-330	2	37
α-helix	335-346	12
β-strand	357-358	2	34
α-helix	359-365	7
α-helix	367-371	5

Chain H: 21 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	39
β-strand	16-21	6	39
β-strand	29-32	4	39
β-strand	35-38	4	40
β-strand	53-54	2	40
α-helix	56-59	4
β-strand	65-68	4	40
α-helix	79-88	10
α-helix	89-94	6
β-strand	103-107	5	39
α-helix	108	1
α-helix	114-125	12
β-strand	131-136	6	39
α-helix	137-144	8
β-strand	150-155	6	41
β-strand	160-166	7	41
β-strand	169-170	2	41
α-helix	172-174	3
β-strand	176-178	3	41
α-helix	182-194	13
α-helix	203-215	13
α-helix	223-230	8
β-strand	238-241	4	42
β-strand	247-250	4	42
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-266	3
α-helix	274-282	9
α-helix	287-294	8
β-strand	297-300	4	41
α-helix	303-305	3
α-helix	309-318	10
β-strand	329-330	2	41
α-helix	338-347	10
α-helix	356	1
β-strand	357-358	2	39
α-helix	359-362	4
α-helix	367-372	6

10 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, G, H, I, J	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Cofilin-2	K, L, M, N, O, P, Q, R	protein	168	Homo sapiens	Q9Y281 (AlphaFold model)

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

>7U8K_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F, G, H, I, J)
XDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVM
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITK
QEYDEAGPSIVHRKCFX

Sequence of entity 2 (K, L, M, N, O, P, Q, R), FASTA

>7U8K_2 Cofilin-2 (chains K, L, M, N, O, P, Q, R)
XMASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGD
IGDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYAS
SKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPLX

Primary citation

Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode. Kraus, J., Russell, R.W., Kudryashova, E. et al. Nat Commun (2022) 13:2114-2114. DOI 10.1038/s41467-022-29595-9 · 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

About this viewer

MolViewer shows 7U8K directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.