3J8I: Near-Atomic Resolution for One State of F-Actin

Near-Atomic Resolution for One State of F-Actin. Determined by electron microscopy at 4.7 Å resolution. Released 14 Jan 2015.

Method: Electron microscopy
Resolution: 4.7 Å
Organism: Oryctolagus cuniculus
Chains: 5
Atoms: 14,800
Mol. weight: 212.74 kDa
Ligands: MG, ADP
Released: 14 Jan 2015

Explore 3J8I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3J8I contains 105 α-helices and 86 β-strands across 5 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 D: 21 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	1
β-strand	16-20	5	1
β-strand	29-32	4	1
β-strand	38	1	2
α-helix	57-60	4
β-strand	65	1	2
β-strand	71-72	2	3
β-strand	75-76	2	3
α-helix	83-88	6
α-helix	89-93	5
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-126	5
β-strand	132-136	5	1
α-helix	137-143	7
β-strand	150-153	4	4
β-strand	160	1	5
β-strand	162-166	5	4
β-strand	169-170	2	4
β-strand	178	1	5
α-helix	182-192	11
α-helix	193-195	3
α-helix	203-209	7
α-helix	212-215	4
α-helix	224-232	9
β-strand	242	1	6
β-strand	246	1	6
α-helix	253-256	4
α-helix	259-262	4
α-helix	274-283	10
α-helix	291-294	4
β-strand	297-299	3	4
α-helix	309-320	12
α-helix	322	1
α-helix	338-342	5
α-helix	343-347	5
β-strand	357	1	1
α-helix	361-364	4
α-helix	367-371	5

Chain E: 20 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	7
β-strand	16-20	5	7
β-strand	29-32	4	7
β-strand	38	1	8
α-helix	57-60	4
β-strand	65	1	8
β-strand	71-72	2	9
β-strand	75-76	2	9
α-helix	83-88	6
α-helix	89-94	6
β-strand	103-107	5	7
α-helix	113-121	9
α-helix	122-126	5
β-strand	132-136	5	7
α-helix	137-143	7
β-strand	150-153	4	10
β-strand	160	1	11
β-strand	162-166	5	10
β-strand	169-170	2	10
β-strand	178	1	11
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-209	7
α-helix	212-215	4
α-helix	224-232	9
β-strand	242	1	12
β-strand	246	1	12
α-helix	253-262	10
α-helix	274-283	10
α-helix	291-294	4
β-strand	297-299	3	10
α-helix	309-320	12
α-helix	322	1
α-helix	338-342	5
α-helix	343-347	5
β-strand	357	1	7
α-helix	361-364	4
α-helix	367-371	5

Chain F: 21 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	13
β-strand	16-20	5	13
β-strand	29-32	4	13
β-strand	38	1	14
α-helix	57-60	4
β-strand	65	1	14
β-strand	71-72	2	15
β-strand	75-76	2	15
α-helix	83-88	6
α-helix	89-93	5
β-strand	103-107	5	13
α-helix	113-121	9
α-helix	122-126	5
β-strand	132-136	5	13
α-helix	137-143	7
β-strand	150-153	4	16
β-strand	162-166	5	16
β-strand	169-170	2	16
α-helix	182-192	11
α-helix	193-195	3
α-helix	203-209	7
α-helix	212-215	4
α-helix	224-232	9
β-strand	242	1	17
β-strand	246	1	17
α-helix	253-256	4
α-helix	259-262	4
α-helix	274-283	10
α-helix	291-295	5
β-strand	297-299	3	16
α-helix	309-320	12
α-helix	322	1
α-helix	338-342	5
α-helix	343-347	5
β-strand	357	1	13
α-helix	361-364	4
α-helix	367-371	5

Chain G: 23 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	18
β-strand	16-20	5	18
β-strand	29-32	4	18
β-strand	38	1	19
α-helix	57-60	4
β-strand	65	1	19
β-strand	71-72	2	20
β-strand	75-76	2	20
α-helix	83-88	6
α-helix	89-94	6
β-strand	103-107	5	18
α-helix	113-121	9
α-helix	122-126	5
β-strand	132-136	5	18
α-helix	137-143	7
β-strand	150-153	4	21
β-strand	160	1	22
β-strand	162-166	5	21
β-strand	169-170	2	21
α-helix	172-174	3
β-strand	178	1	22
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-209	7
α-helix	212-215	4
α-helix	224-232	9
β-strand	242	1	23
β-strand	246	1	23
α-helix	253-256	4
α-helix	259-262	4
α-helix	274-283	10
α-helix	291-295	5
β-strand	297-299	3	21
α-helix	309-320	12
α-helix	322	1
α-helix	338-342	5
α-helix	343-347	5
α-helix	353-355	3
β-strand	357	1	18
α-helix	361-364	4
α-helix	367-371	5

Chain H: 20 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	24
β-strand	16-20	5	24
β-strand	29-32	4	24
β-strand	38	1	25
α-helix	57-60	4
β-strand	65	1	25
β-strand	71-72	2	26
β-strand	75-76	2	26
α-helix	83-88	6
α-helix	89-94	6
β-strand	103-107	5	24
α-helix	113-121	9
α-helix	122-126	5
β-strand	132-136	5	24
α-helix	137-143	7
β-strand	150-153	4	27
β-strand	162-166	5	27
β-strand	169-170	2	27
α-helix	182-192	11
α-helix	193-196	4
α-helix	203-209	7
α-helix	212-215	4
α-helix	224-232	9
β-strand	242	1	28
β-strand	246	1	28
α-helix	253-262	10
α-helix	274-283	10
α-helix	291-294	4
β-strand	297-299	3	27
α-helix	309-320	12
α-helix	322	1
α-helix	338-342	5
α-helix	343-347	5
β-strand	357	1	24
α-helix	361-364	4
α-helix	367-371	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	D, E, F, G, H	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)

Sequence of entity 1 (D, E, F, G, H), FASTA

>3J8I_1 Actin, alpha skeletal muscle (chains D, E, F, G, H)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Ligands and cofactors

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

Primary citation

Near-atomic resolution for one state of f-actin. Galkin, V.E., Orlova, A., Vos, M.R. et al. Structure (2015) 23:173-182. DOI 10.1016/j.str.2014.11.006 · 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

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3J8I is part of these collections:

Motor proteins and the cytoskeleton

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