4PKG: Actin, alpha skeletal muscle

Complex of ATP-actin With the N-terminal Actin-Binding Domain of Tropomodulin. Determined by X-ray diffraction at 1.8 Å resolution. Released 30 Jul 2014.

Method: X-ray diffraction
Resolution: 1.8 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 2
Atoms: 4,904
Mol. weight: 63.56 kDa
Ligands: CA, ATP
Released: 30 Jul 2014

Explore 4PKG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PKG contains 36 α-helices and 26 β-strands across 2 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: 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
α-helix	39-40	2
β-strand	53-54	2	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	79-88	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	137-144	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	182-196	15
α-helix	203-205	3
α-helix	206-216	11
α-helix	223-232	10
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-262	10
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	4
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain G: 11 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	57-61	5
β-strand	67-74	8	6
β-strand	77-80	4	6
α-helix	81-82	2
α-helix	83-85	3
β-strand	88-90	3	7
β-strand	94-102	9	6
α-helix	107	1
β-strand	108-116	9	6
α-helix	122-138	17
α-helix	143	1
β-strand	144-149	6	6
α-helix	155-159	5
β-strand	166-168	3	7
α-helix	172-174	3
α-helix	1064-1076	13
α-helix	1084-1087	4
α-helix	1094-1096	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Gelsolin,Tropomodulin-1 chimera	G	protein	186	Homo sapiens	P06396 (AlphaFold model), P28289 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4PKG_1 Actin, alpha skeletal muscle (chains A)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (G), FASTA

>4PKG_2 Gelsolin,Tropomodulin-1 chimera (chains G)
MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD
LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG
VASGFGGSGGSGGSQKDQTTKAPTGPFKREELLDHLEKQAKEFKDREDLVPYTGEKRGKV
WVPKQK

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	3
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1

Primary citation

Actin cytoskeleton. Mechanism of actin filament pointed-end capping by tropomodulin. Rao, J.N., Madasu, Y., Dominguez, R. Science (2014) 345:463-467. DOI 10.1126/science.1256159 · 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

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