7SX9: Actin, alpha skeletal muscle

T-Plastin-F-actin complex, anti-parallel bundled state. Determined by electron microscopy at 10.0 Å resolution. Released 31 Aug 2022.

Method: Electron microscopy
Resolution: 10.0 Å
Organisms: Gallus gallus, Homo sapiens
Chains: 7
Atoms: 21,036
Mol. weight: 326.27 kDa
Ligands: MG, ADP
Released: 31 Aug 2022

Explore 7SX9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7SX9 contains 192 α-helices and 116 β-strands across 7 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	6
β-strand	16-21	6	6
β-strand	29-32	4	6
β-strand	35-38	4	7
β-strand	41-42	2	8
β-strand	53	1	7
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	7
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	6
α-helix	113-125	13
β-strand	131-136	6	6
α-helix	137-145	9
β-strand	150-155	6	10
β-strand	160-166	7	10
β-strand	169-170	2	10
α-helix	172-174	3
β-strand	176-178	3	10
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	11
β-strand	247-250	4	11
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	10
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	10
α-helix	333-337	5
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain B: 26 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	1	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	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	1
α-helix	137-144	8
β-strand	150-155	6	4
β-strand	160-166	7	4
β-strand	169-170	2	4
α-helix	172-174	3
β-strand	176-178	3	4
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	5
β-strand	247-250	4	5
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	4
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	333-337	5
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain C: 28 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	12
β-strand	16-21	6	12
β-strand	29-32	4	12
β-strand	35-38	4	13
α-helix	47-49	3
β-strand	53	1	13
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	13
β-strand	71-72	2	14
β-strand	75-76	2	14
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	12
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	12
α-helix	137-143	7
β-strand	150-155	6	8
β-strand	160-166	7	8
β-strand	169-170	2	8
α-helix	172-174	3
β-strand	176-178	3	8
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	15
β-strand	247-250	4	15
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	8
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	8
α-helix	333-337	5
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	12
α-helix	359-365	7
α-helix	366-369	4
α-helix	370-373	4

Chain D: 33 helices, 0 β-strands

Element	Residues	Length
α-helix	127-137	11
α-helix	143-145	3
α-helix	156-161	6
α-helix	164-168	5
α-helix	169-171	3
α-helix	180-183	4
α-helix	195-201	7
α-helix	216-219	4
α-helix	224-238	15
α-helix	270-278	9
α-helix	279-282	4
α-helix	299-309	11
α-helix	333-336	4
α-helix	338-345	8
α-helix	355-360	6
α-helix	363-373	11
α-helix	398-410	13
α-helix	419-422	4
α-helix	423-425	3
α-helix	427-435	9
α-helix	442-444	3
α-helix	446-447	2
α-helix	455-471	17
α-helix	483-488	6
α-helix	491-512	22
α-helix	522-531	10
α-helix	532-534	3
α-helix	547-550	4
α-helix	553-559	7
α-helix	564-566	3
α-helix	582-596	15
α-helix	604-608	5
α-helix	612-626	15

Chain E: 27 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	41-42	2	23
α-helix	47-49	3
β-strand	53	1	22
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	22
β-strand	71-72	2	24
β-strand	75-76	2	24
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
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	25
β-strand	160-166	7	25
β-strand	169-170	2	25
α-helix	172-174	3
β-strand	176-178	3	25
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	26
β-strand	247-250	4	26
α-helix	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	25
α-helix	302-305	4
α-helix	309-320	12
α-helix	326-327	2
β-strand	329-330	2	25
α-helix	333-337	5
α-helix	338-348	11
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 G: 25 helices, 19 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	53	1	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	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-125	13
β-strand	131-136	6	16
α-helix	137-144	8
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	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
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	274-283	10
α-helix	290-295	6
β-strand	297-300	4	19
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	333-337	5
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain H: 27 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	27
β-strand	16-21	6	27
β-strand	29-32	4	27
β-strand	35-38	4	28
α-helix	47-49	3
β-strand	53	1	28
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	28
β-strand	71-72	2	29
β-strand	75-76	2	29
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	27
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	27
α-helix	137-144	8
β-strand	150-155	6	23
β-strand	160-166	7	23
β-strand	169-170	2	23
α-helix	172-174	3
β-strand	176-178	3	23
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	30
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	23
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	23
α-helix	333-337	5
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	27
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, E, G, H	protein	377	Gallus gallus	P68139 (AlphaFold model)
Plastin-3	D	protein	630	Homo sapiens	P13797 (AlphaFold model)

Sequence of entity 1 (A, B, C, E, G, H), FASTA

>7SX9_1 Actin, alpha skeletal muscle (chains A, B, C, E, G, H)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (D), FASTA

>7SX9_2 Plastin-3 (chains D)
MDEMATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKL
MLDGDRNKDGKISFDEFVYIFQEVKSSDIAKTFRKAINRKEGICALGGTSELSSEGTQHS
YSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE
RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLF
ADIELSRNEALAALLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSK
AYFHLLNQIAPKGQKEGEPRIDINMSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVS
GNPKLNLAFVANLFNKYPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLY
ADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKHPAKFSLVG
IGGQDLNDGNQTLTLALVWQLMRRYTLNVLEDLGDGQKANDDIIVNWVNRTLSEAGKSTS
IQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGARV
YALPEDLVEVKPKMVMTVFACLMGRGMKRV

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	6
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6

Primary citation

Structural mechanism for bidirectional actin cross-linking by T-plastin. Mei, L., Reynolds, M.J., Garbett, D. et al. Proc Natl Acad Sci U S A (2022) 119:e2205370119-e2205370119. DOI 10.1073/pnas.2205370119 · 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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