3CJC: Actin, alpha skeletal muscle

Actin dimer cross-linked by V. cholerae MARTX toxin and complexed with DNase I and Gelsolin-segment 1. Determined by X-ray diffraction at 3.9 Å resolution. Released 25 Mar 2008.

Method: X-ray diffraction
Resolution: 3.9 Å
Organisms: Oryctolagus cuniculus, Bos taurus, Homo sapiens
Chains: 3
Atoms: 6,029
Mol. weight: 86.85 kDa
Ligands: ATP, CA
Released: 25 Mar 2008

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

Secondary structure: helices and β-sheets

3CJC contains 41 α-helices and 44 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, 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	42-44	3	3
β-strand	53-54	2	2
α-helix	56-60	5
β-strand	65-68	4	2
β-strand	71-72	2	4
β-strand	75-76	2	4
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	132-136	5	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	182-196	15
α-helix	203-206	4
α-helix	208-216	9
α-helix	223-230	8
β-strand	238-241	4	6
β-strand	247-250	4	6
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-295	6
β-strand	297-300	4	5
α-helix	302-304	3
α-helix	309-320	12
β-strand	329	1	5
α-helix	338-348	11
α-helix	351-354	4
α-helix	359-365	7
α-helix	366-371	6

Chain D: 12 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	2-11	10	3
α-helix	13-17	5
α-helix	19-29	11
β-strand	34-40	7	3
α-helix	46-55	10
β-strand	64-67	4	3
β-strand	71	1	7
β-strand	78	1	7
β-strand	79-84	6	3
β-strand	90-96	7	8
β-strand	114-119	6	8
β-strand	127-132	6	8
α-helix	140-145	6
α-helix	147-157	11
β-strand	163-168	6	8
α-helix	178-181	4
α-helix	185-188	4
β-strand	192-194	3	8
β-strand	203	1	9
β-strand	212-217	6	8
α-helix	219-224	6
β-strand	225	1	10
α-helix	226	1
β-strand	231	1	3
α-helix	235-239	5
α-helix	243-249	7
β-strand	252	1	9
α-helix	253-254	2
β-strand	255-258	4	3
β-strand	259	1	10

Chain G: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	6-10	5
β-strand	18-22	5	11
β-strand	27-29	3	11
α-helix	30-31	2
α-helix	32-34	3
β-strand	37-39	3	12
β-strand	43-51	9	11
β-strand	57-65	9	11
α-helix	71-87	17
β-strand	92-98	7	11
α-helix	104-109	6
β-strand	115-117	3	12
α-helix	121-123	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Deoxyribonuclease-1	D	protein	260	Bos taurus	P00639 (AlphaFold model)
Gelsolin	G	protein	125	Homo sapiens	P06396 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3CJC_1 Actin, alpha skeletal muscle (chains A)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (D), FASTA

>3CJC_2 Deoxyribonuclease-1 (chains D)
LKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDP
NTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSS
HSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQ
WSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYG
LSNEMALAISDHYPVEVTLT

Sequence of entity 3 (G), FASTA

>3CJC_3 Gelsolin (chains G)
MVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPTNLYGDFFTGDAYVILKTVQLRNGNLQYD
LHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESATFLGYFKSGLKYKKGG
VASGF

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1
CA	Calcium ion	Ca	2

Water and common crystallization additives (SO4) are not listed.

Primary citation

Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin. Kudryashov, D.S., Durer, Z.A., Ytterberg, A.J. et al. Proc Natl Acad Sci U S A (2008) 105:18537-18542. DOI 10.1073/pnas.0808082105 · 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

About this viewer

MolViewer shows 3CJC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.