8V30: Actin, gamma-enteric smooth muscle

Smooth Muscle Gamma Actin (ACTG2) Filament Mutant R40C. Determined by electron microscopy at 2.54 Å resolution. Released 1 May 2024.

Method: Electron microscopy
Resolution: 2.54 Å
Organisms: Homo sapiens, synthetic construct
Chains: 10
Atoms: 14,910
Mol. weight: 215.71 kDa
Ligands: MG, ADP
Released: 1 May 2024

Explore 8V30 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8V30 contains 115 α-helices and 98 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 A: 24 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
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	53-54	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	79-87	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	137-145	9
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	182-192	11
α-helix	193-195	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	274-283	10
α-helix	287-294	8
β-strand	297-300	4	4
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	369-371	3

Chain B: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
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	53-54	2	7
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	7
β-strand	71-72	2	8
β-strand	75-76	2	8
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	9
β-strand	160-166	7	9
β-strand	169-170	2	9
α-helix	172-174	3
β-strand	176-178	3	9
α-helix	182-192	11
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	9
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	369-371	3

Chains C and E: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	11
β-strand	16-21	6	11
β-strand	29-32	4	11
β-strand	35-38	4	12
β-strand	42	1	4
β-strand	53-54	2	12
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	12
β-strand	71-72	2	13
β-strand	75-76	2	13
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	11
α-helix	113-125	13
β-strand	131-136	6	11
α-helix	137-145	9
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	182-192	11
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	15
β-strand	247-250	4	15
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	14
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	338-347	10
α-helix	350-352	3
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	369-371	3

Chain D: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	5-7	3
β-strand	8-12	5	16
β-strand	16-21	6	16
β-strand	29-32	4	16
β-strand	35-38	4	17
β-strand	42	1	9
β-strand	53-54	2	17
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	17
β-strand	71-72	2	18
β-strand	75-76	2	18
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-125	13
β-strand	131-136	6	16
α-helix	137-145	9
β-strand	150-155	6	19
β-strand	160-166	7	19
β-strand	169-170	2	19
α-helix	172-174	3
β-strand	176-178	3	19
α-helix	182-192	11
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	20
β-strand	247-250	4	20
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	19
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	338-347	10
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	369-371	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, gamma-enteric smooth muscle	A, B, C, D, E	protein	376	Homo sapiens	P63267 (AlphaFold model)
Phalloidin	F, G, H, I, J	protein	7	synthetic construct

Sequence of entity 1 (A, B, C, D, E), FASTA

>8V30_1 Actin, gamma-enteric smooth muscle (chains A, B, C, D, E)
MCEEETTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPCHQGVMVGMGQKDSYVGDEAQ
SKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKM
TQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLD
LAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKS
YELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVL
SGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISK
PEYDEAGPSIVHRKCF

Sequence of entity 2 (F, G, H, I, J), FASTA

>8V30_2 Phalloidin (chains F, G, H, I, J)
WXATCPA

Ligands and cofactors

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

Primary citation

Molecular mechanisms linking missense ACTG2 mutations to visceral myopathy. Ceron, R.H., Baez-Cruz, F.A., Palmer, N.J. et al. Sci Adv (2024) 10:eadn6615-eadn6615. DOI 10.1126/sciadv.adn6615 · PubMed

Other PDB entries of the same protein (UniProt P63267 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8V2O 2.45 Å, Cryo-EM Structure of Wildtype Smooth Muscle Gamma Actin (ACTG2)
6JAT 2.71 Å, Crystal structure of SETD3 bound to Actin peptide and SFG
8V2Z 2.72 Å, Cryo-EM Structure of Smooth Muscle Gamma Actin (ACTG2) Mutant R257C

Browse structure collections

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