6NAS: Actin, alpha skeletal muscle

Ternary Complex of Ac-Alpha-Actin with Profilin and AcCoA-NAA80. Determined by X-ray diffraction at 2.9 Å resolution. Released 29 Jan 2020.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 3
Atoms: 5,529
Mol. weight: 85.14 kDa
Ligands: CA, ATP, ACO, LAB
Released: 29 Jan 2020

Explore 6NAS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6NAS contains 38 α-helices and 38 β-strands across 3 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: 23 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	2-7	6
β-strand	8-12	5	1
β-strand	16-21	6	1
β-strand	22	1	2
β-strand	24	1	2
β-strand	29-32	4	1
β-strand	35-38	4	3
β-strand	53-54	2	3
α-helix	55-60	6
α-helix	62-64	3
β-strand	65-68	4	3
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	79-87	9
α-helix	88-94	7
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	5
β-strand	160-166	7	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	176-178	3	5
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	6
β-strand	247-250	4	6
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	5
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	5
α-helix	338-348	11
α-helix	350-352	3
α-helix	356	1
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	369-373	5

Chain N: 10 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	83-86	4	7
α-helix	87-89	3
α-helix	91-93	3
α-helix	94-104	11
α-helix	109-117	9
β-strand	125-131	7	7
β-strand	141-151	11	7
β-strand	154-165	12	7
α-helix	167-169	3
α-helix	174-188	15
β-strand	193-198	6	7
α-helix	202-207	6
β-strand	211-212	2	7
β-strand	218	1	7
α-helix	219-221	3
α-helix	264-266	3
α-helix	291-293	3
β-strand	294	1	8
β-strand	300	1	8
β-strand	302-307	6	7

Chain P: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	4-11	8
β-strand	16-23	8	9
β-strand	29-33	5	9
α-helix	39-41	3
α-helix	44-51	8
α-helix	57-61	5
β-strand	63-65	3	9
β-strand	68-76	9	9
β-strand	84-89	6	9
β-strand	99-104	6	9
β-strand	108-114	7	9
α-helix	120-136	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A	protein	375	Oryctolagus cuniculus	P68135 (AlphaFold model)
N-alpha-acetyltransferase 80	N	protein	235	Homo sapiens	Q93015 (AlphaFold model)
Profilin-1	P	protein	140	Homo sapiens	P07737 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6NAS_1 Actin, alpha skeletal muscle (chains A)
XEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 2 (N), FASTA

>6NAS_2 N-alpha-acetyltransferase 80 (chains N)
AGHMSLAELTLEPVHRRPELLDACADLINDQWPRSRTSRLHSLGQSSDAFPLCLMLLSPH
PTLEAAPVVVGHARLSRVLNQPQSLLVETVVVARALRGRGFGRRLMEGLEVFARARGFRK
LHLTTHDQVHFYTHLGYQLGEPVQGLVFTSRRLPATLLNAFPTAPSPRPPRKAPNLTAQA
APRGPKGPPLPPPPPLPECLTISPPVPSGPPSKSLLETQYQNVRGRPIFWMEKDI

Sequence of entity 3 (P), FASTA

>6NAS_3 Profilin-1 (chains P)
MAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFY
VNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVH
GGLINKKCYEMASHLRRSQY

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
ACO	Acetyl coenzyme *a	C23 H38 N7 O17 P3 S	1
LAB	Latrunculin B	C20 H29 N O5 S	1

Water and common crystallization additives (GOL, MES) are not listed.

Primary citation

Mechanism of actin N-terminal acetylation. Rebowski, G., Boczkowska, M., Drazic, A. et al. Sci Adv (2020) 6:eaay8793-eaay8793. DOI 10.1126/sciadv.aay8793 · 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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