7SXA: Plastin-3

T-Plastin-F-actin complex, pre-bundling intermediate state. Determined by electron microscopy at 6.87 Å resolution. Released 31 Aug 2022.

Method: Electron microscopy
Resolution: 6.87 Å
Organisms: Homo sapiens, Gallus gallus
Chains: 4
Atoms: 11,272
Mol. weight: 198.58 kDa
Ligands: ADP, MG
Released: 31 Aug 2022

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

Secondary structure: helices and β-sheets

7SXA contains 100 α-helices and 58 β-strands across 4 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: 21 helices, 0 β-strands

Element	Residues	Length
α-helix	292-295	4
α-helix	300-309	10
α-helix	328-330	3
α-helix	333-347	15
α-helix	356-359	4
α-helix	363-375	13
α-helix	384-387	4
α-helix	398-409	12
α-helix	415-416	2
α-helix	426-435	10
α-helix	442-444	3
α-helix	456-468	13
α-helix	485-488	4
α-helix	491-513	23
α-helix	518-520	3
α-helix	521-533	13
α-helix	549-551	3
α-helix	552-562	11
α-helix	579-596	18
α-helix	606-609	4
α-helix	616-625	10

Chain B: 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
α-helix	47-49	3
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	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-295	6
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	338-347	10
α-helix	350-354	5
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain C: 25 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	113-125	13
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	272-273	2
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	4
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	333-337	5
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	369-373	5

Chain D: 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	88-94	7
α-helix	98-100	3
β-strand	103-107	5	12
α-helix	113-121	9
α-helix	122-127	6
β-strand	131-136	6	12
α-helix	137-145	9
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	253-259	7
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-295	6
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	338-347	10
α-helix	350-354	5
β-strand	357-358	2	12
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>7SXA_1 Plastin-3 (chains A)
MDEMATTQISKDELDELKEAFAKVDLNSNGFICDYELHELFKEANMPLPGYKVREIIQKL
MLDGDRNKDGKISFDEFVYIFQEVKSSDIAKTFRKAINRKEGICALGGTSELSSEGTQHS
YSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE
RAINKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLF
ADIELSRNEALAALLRDGETLEELMKLSPEELLLRWANFHLENSGWQKINNFSADIKDSK
AYFHLLNQIAPKGQKEGEPRIDINMSGFNETDDLKRAESMLQQADKLGCRQFVTPADVVS
GNPKLNLAFVANLFNKYPALTKPENQDIDWTLLEGETREERTFRNWMNSLGVNPHVNHLY
ADLQDALVILQLYERIKVPVDWSKVNKPPYPKLGANMKKLENCNYAVELGKHPAKFSLVG
IGGQDLNDGNQTLTLALVWQLMRRYTLNVLEDLGDGQKANDDIIVNWVNRTLSEAGKSTS
IQSFKDKTISSSLAVVDLIDAIQPGCINYDLVKSGNLTEDDKHNNAKYAVSMARRIGARV
YALPEDLVEVKPKMVMTVFACLMGRGMKRV

Sequence of entity 2 (B, C, D), FASTA

>7SXA_2 Actin, alpha skeletal muscle (chains B, C, D)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	3
MG	Magnesium ion	Mg	3

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 P13797 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1AOA 2.4 Å, N-terminal actin-crosslinking domain from human fimbrin
7R94 2.6 Å, T-Plastin-F-actin complex
7SX8 9.0 Å, T-Plastin-F-actin complex, parallel bundled state
7SX9 10.0 Å, T-Plastin-F-actin complex, anti-parallel bundled state
1WJO Solution structure of the forth CH domain from human plastin 3 T-isoform

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