8UZ0: Actin, alpha skeletal muscle

Straight actin filament from Arp2/3 branch junction sample (ADP). Determined by electron microscopy at 2.8 Å resolution. Released 31 Jan 2024.

Method: Electron microscopy
Resolution: 2.8 Å
Organism: Oryctolagus cuniculus
Chains: 9
Atoms: 26,433
Mol. weight: 377.71 kDa
Ligands: MG, ADP
Released: 31 Jan 2024

Explore 8UZ0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8UZ0 contains 210 α-helices and 178 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 J: 22 helices, 19 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	55-61	7
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
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	4
β-strand	160-166	7	4
β-strand	169-170	2	4
β-strand	176-178	3	4
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-229	7
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	287-295	9
β-strand	297-300	4	4
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	333-336	4
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	1
α-helix	359-362	4
α-helix	367-372	6

Chain K: 21 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	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	56-61	6
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	89-93	5
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	182-195	14
α-helix	203-216	14
α-helix	223-231	9
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	274-284	11
α-helix	287-295	9
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	359-362	4
α-helix	369-373	5

Chain L: 26 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	56-61	6
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	182-194	13
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	15
α-helix	242	1
β-strand	247-250	4	15
α-helix	253-256	4
α-helix	258-261	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	14
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	11
α-helix	359-362	4
α-helix	367-369	3
α-helix	370-373	4

Chain M: 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	56-61	6
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
β-strand	103-107	5	16
α-helix	113-121	9
α-helix	122-126	5
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
β-strand	176-178	3	19
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	20
β-strand	247-250	4	20
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	19
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	16
α-helix	359-362	4
α-helix	367-369	3
α-helix	370-373	4

Chain N: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	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	79-88	10
α-helix	89-93	5
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	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	25
β-strand	247-250	4	25
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	287-294	8
β-strand	297-300	4	24
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	24
α-helix	335-337	3
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	21
α-helix	359-362	4
α-helix	369-373	5

Chain O: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	26
β-strand	15-21	7	26
β-strand	29-33	5	26
β-strand	35-38	4	27
β-strand	41-42	2	19
β-strand	53-54	2	27
α-helix	56-61	6
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	79-87	9
α-helix	88-93	6
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
α-helix	172-174	3
β-strand	176-178	3	29
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	30
α-helix	242	1
β-strand	247-250	4	30
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	29
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	29
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	26
α-helix	359-363	5
α-helix	367-369	3
α-helix	370-373	4

Chain P: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	31
β-strand	16-21	6	31
β-strand	29-32	4	31
β-strand	35-38	4	32
β-strand	41-42	2	24
β-strand	53-54	2	32
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	32
β-strand	71-72	2	33
β-strand	75-76	2	33
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	31
α-helix	113-125	13
β-strand	131-136	6	31
α-helix	137-145	9
β-strand	150-155	6	34
β-strand	160-166	7	34
β-strand	169-170	2	34
α-helix	172-174	3
β-strand	176-178	3	34
α-helix	182-193	12
α-helix	194-196	3
α-helix	205-216	12
α-helix	223-231	9
β-strand	238-241	4	35
β-strand	247-250	4	35
α-helix	253-256	4
α-helix	258-261	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	34
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	34
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	31
α-helix	359-362	4
α-helix	369-373	5

Chain Q: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	36
β-strand	16-21	6	36
β-strand	29-32	4	36
β-strand	35-38	4	37
β-strand	41-42	2	29
β-strand	53-54	2	37
α-helix	56-61	6
α-helix	62-64	3
β-strand	65-68	4	37
β-strand	71-72	2	38
β-strand	75-76	2	38
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	36
α-helix	113-125	13
β-strand	131-136	6	36
α-helix	137-145	9
β-strand	150-155	6	39
β-strand	160-166	7	39
β-strand	169-170	2	39
β-strand	176-178	3	39
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	40
α-helix	242	1
β-strand	247-250	4	40
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-284	11
α-helix	287-295	9
β-strand	297-300	4	39
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	39
α-helix	338-346	9
α-helix	351-354	4
β-strand	357-358	2	36
α-helix	359-362	4
α-helix	367-369	3
α-helix	370-373	4

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	J, K, L, M, N, O, P, Q, R	protein	372	Oryctolagus cuniculus	P68139 (AlphaFold model)

Sequence of entity 1 (J, K, L, M, N, O, P, Q, R), FASTA

>8UZ0_1 Actin, alpha skeletal muscle (chains J, K, L, M, N, O, P, Q, R)
ETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRG
ILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIM
FETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGR
DLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELP
DGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGT
TMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYD
EAGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	9
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	9

Primary citation

Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Chavali, S.S., Chou, S.Z., Cao, W. et al. Nat Commun (2024) 15:2059-2059. DOI 10.1038/s41467-024-46179-x · PubMed

Other PDB entries of the same protein (UniProt P68139 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7W4Z 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (AMPPNP-form)
7W50 1.15 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-Pi-form)
7W51 1.2 Å, Crystal structure of fragmin domain-1 in complex with actin (ADP-form)
9L2N 1.7 Å, Crystal structure of Cytochalasin D bound to a filamentous conformation actin
7W52 2.0 Å, Crystal structure of fragmin domain-1 (15-160) in complex with actin
1MDU 2.2 Å, Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1…
8D13 2.43 Å, Helical ADP-F-actin
8D14 2.51 Å, Helical ADP-Pi-F-actin
7R94 2.6 Å, T-Plastin-F-actin complex
8C4E 2.6 Å, F-actin decorated by SipA426-685
9JW0 2.69 Å, Structure of the N-terminal 3 domains (V1-V3) villin bound to actin
7YNE 2.7 Å, Crystal structure of fragmin domain-1 (1-160) in complex with G-form actin

Browse structure collections

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