7SX8: Actin, alpha skeletal muscle

T-Plastin-F-actin complex, parallel bundled state. Determined by electron microscopy at 9.0 Å resolution. Released 31 Aug 2022.

Method: Electron microscopy
Resolution: 9.0 Å
Organisms: Gallus gallus, Homo sapiens
Chains: 7
Atoms: 21,036
Mol. weight: 326.27 kDa
Ligands: MG, ADP
Released: 31 Aug 2022

Explore 7SX8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7SX8 contains 172 α-helices and 127 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: 22 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	16
β-strand	16	1	17
β-strand	18-21	4	16
β-strand	32	1	17
β-strand	35-36	2	18
β-strand	38	1	19
β-strand	41-42	2	7
β-strand	53-54	2	18
α-helix	56-59	4
β-strand	65	1	19
β-strand	68	1	18
β-strand	71-72	2	20
β-strand	75-76	2	20
α-helix	79-91	13
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	16
α-helix	137-144	8
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	183-192	10
α-helix	193-196	4
α-helix	203-205	3
α-helix	206-216	11
α-helix	223-232	10
β-strand	238-241	4	22
β-strand	247-250	4	22
α-helix	256-262	7
α-helix	264-266	3
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	21
α-helix	309-320	12
β-strand	330	1	21
α-helix	335-337	3
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	369-373	5

Chain B: 21 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-11	4	9
β-strand	16-19	4	9
β-strand	29-32	4	9
β-strand	35	1	10
β-strand	36	1	11
β-strand	38	1	12
β-strand	53	1	11
α-helix	56-60	5
α-helix	62-64	3
β-strand	65	1	12
β-strand	68	1	10
β-strand	71	1	13
β-strand	76	1	13
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	9
α-helix	113-125	13
β-strand	134-136	3	9
α-helix	137-144	8
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	183-192	10
α-helix	193-196	4
α-helix	204-216	13
α-helix	223-232	10
β-strand	238-241	4	15
β-strand	247-250	4	15
α-helix	258-260	3
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	14
α-helix	303-305	3
α-helix	309-319	11
β-strand	330	1	14
α-helix	338-347	10
α-helix	359-365	7
α-helix	369-373	5

Chain C: 23 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16-19	4	1
β-strand	29-32	4	1
β-strand	35	1	2
β-strand	36	1	3
β-strand	38	1	4
β-strand	53	1	3
α-helix	57-60	4
α-helix	62-64	3
β-strand	65	1	4
β-strand	68	1	2
β-strand	71	1	5
β-strand	76	1	5
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-127	6
β-strand	131-136	6	1
α-helix	137-141	5
β-strand	151-153	3	6
β-strand	160-163	4	6
β-strand	165-166	2	7
β-strand	169-170	2	7
α-helix	172-174	3
β-strand	176-178	3	6
α-helix	183-193	11
α-helix	203-205	3
α-helix	206-216	11
α-helix	223-232	10
β-strand	238-241	4	8
β-strand	247-250	4	8
α-helix	253-256	4
α-helix	258-260	3
α-helix	264-266	3
α-helix	274-283	10
α-helix	291-294	4
β-strand	297-299	3	6
α-helix	310-320	11
β-strand	330	1	6
α-helix	335-337	3
α-helix	338-347	10
α-helix	351-353	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	369-373	5

Chain D: 32 helices, 0 β-strands

Element	Residues	Length
α-helix	127-137	11
α-helix	141-145	5
α-helix	156-161	6
α-helix	164-168	5
α-helix	169-172	4
α-helix	180-183	4
α-helix	195-201	7
α-helix	218-220	3
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	338-341	4
α-helix	355-360	6
α-helix	363-373	11
α-helix	374-376	3
α-helix	398-410	13
α-helix	419-422	4
α-helix	427-435	9
α-helix	442-444	3
α-helix	446-447	2
α-helix	455-471	17
α-helix	483-487	5
α-helix	491-512	22
α-helix	522-531	10
α-helix	547-549	3
α-helix	553-562	10
α-helix	564-566	3
α-helix	582-596	15
α-helix	604-608	5
α-helix	612-626	15

Chain E: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-10	3	34
β-strand	11-12	2	35
β-strand	16-19	4	35
β-strand	21	1	34
β-strand	29-32	4	35
β-strand	35-38	4	36
β-strand	41-42	2	26
β-strand	53	1	36
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	36
β-strand	71-72	2	37
β-strand	75-76	2	37
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	34
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	34
α-helix	137-144	8
β-strand	150-155	6	38
β-strand	160-166	7	38
β-strand	169-170	2	38
α-helix	172-174	3
β-strand	176-178	3	38
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	39
β-strand	247-250	4	39
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-295	9
β-strand	297-300	4	38
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	38
α-helix	335-337	3
α-helix	338-348	11
α-helix	351-354	4
β-strand	357-358	2	34
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain G: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-10	3	28
β-strand	11-12	2	29
β-strand	16-19	4	29
β-strand	21	1	28
β-strand	29-32	4	29
β-strand	35-38	4	30
β-strand	53	1	30
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	30
β-strand	71-72	2	31
β-strand	75-76	2	31
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	28
α-helix	113-125	13
β-strand	132-136	5	28
α-helix	137-145	9
β-strand	150-155	6	32
β-strand	160-166	7	32
β-strand	169-170	2	32
α-helix	172-174	3
β-strand	176-178	3	32
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	33
β-strand	247-250	4	33
α-helix	253-259	7
α-helix	264-267	4
α-helix	271-273	3
α-helix	274-283	10
α-helix	287-295	9
β-strand	297-300	4	32
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	32
α-helix	335-337	3
α-helix	338-348	11
α-helix	351-354	4
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain H: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	23
β-strand	16-21	6	23
β-strand	29-32	4	23
β-strand	35-38	4	24
β-strand	53	1	24
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	24
β-strand	71-72	2	25
β-strand	75-76	2	25
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	23
α-helix	113-127	15
β-strand	132-136	5	23
α-helix	137-145	9
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	182-193	12
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	27
β-strand	247-250	4	27
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-295	9
β-strand	297-300	4	26
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	26
α-helix	335-337	3
α-helix	338-348	11
α-helix	351-354	4
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

>7SX8_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

>7SX8_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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