7CCC: Actin, alpha skeletal muscle

The structure of the actin filament uncapping complex mediated by twinfilin. Determined by X-ray diffraction at 3.2 Å resolution. Released 3 Feb 2021.

Method: X-ray diffraction
Resolution: 3.2 Å
Organisms: Oryctolagus cuniculus, Homo sapiens, Mus musculus
Chains: 5
Atoms: 12,626
Mol. weight: 189.15 kDa
Ligands: CA, ADP
Released: 3 Feb 2021

Explore 7CCC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CCC contains 88 α-helices and 69 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: 20 helices, 17 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	53-54	2	2
α-helix	56-60	5
β-strand	65-68	4	2
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	3
β-strand	160-166	7	3
β-strand	169-170	2	3
α-helix	172-174	3
β-strand	176-178	3	3
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	4
β-strand	247-250	4	4
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	3
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	3
α-helix	335-348	14
α-helix	350-355	6
β-strand	357-358	2	1
α-helix	359-365	7

Chain B: 22 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	9	1	5
α-helix	11-20	10
β-strand	27-33	7	5
β-strand	36-43	8	5
α-helix	49-57	9
α-helix	58-60	3
β-strand	67-76	10	5
β-strand	81-88	8	5
α-helix	95-103	9
α-helix	105-112	8
α-helix	114-116	3
β-strand	117-123	7	5
α-helix	126-129	4
α-helix	131-141	11
α-helix	144-146	3
α-helix	149-166	18
α-helix	171-173	3
α-helix	175-177	3
α-helix	180-181	2
β-strand	182	1	6
α-helix	183	1
α-helix	184-194	11
β-strand	200-206	7	6
β-strand	211-216	6	6
α-helix	225-228	4
β-strand	235-245	11	6
β-strand	248-258	11	6
α-helix	266-281	16
α-helix	282-286	5
β-strand	291-297	7	6
α-helix	300-302	3
α-helix	305-312	8
α-helix	314-321	8
α-helix	323-326	4

Chain C: 12 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	10-22	13
α-helix	24-25	2
α-helix	29-40	12
α-helix	43-49	7
α-helix	51-60	10
β-strand	64-65	2	7
α-helix	66-67	2
β-strand	74-75	2	7
β-strand	81	1	8
β-strand	86-89	4	8
β-strand	94-99	6	8
β-strand	104-110	7	8
α-helix	118-135	18
β-strand	136	1	9
β-strand	139-148	10	10
β-strand	151-164	14	10
β-strand	169-180	12	10
β-strand	186-198	13	10
β-strand	202-216	15	10
α-helix	221-249	29
α-helix	250-254	5
α-helix	255-258	4
α-helix	268-270	3
α-helix	271-274	4

Chain D: 9 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	3-15	13
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
β-strand	48-51	4	11
β-strand	58-61	4	11
β-strand	66-67	2	12
β-strand	70-72	3	12
β-strand	79-80	2	12
α-helix	91-111	21
β-strand	116-123	8	10
β-strand	128-137	10	10
β-strand	145-158	14	10
β-strand	164-181	18	10
β-strand	185-202	18	10
α-helix	209-227	19
α-helix	228-232	5
α-helix	233-243	11
β-strand	244	1	9

Chain E: 25 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	13
β-strand	16-21	6	13
β-strand	29-32	4	13
β-strand	35-37	3	14
β-strand	53-54	2	14
α-helix	56-60	5
β-strand	66-68	3	14
α-helix	72-74	3
α-helix	79-88	10
α-helix	89-94	6
α-helix	98-100	3
β-strand	103-107	5	13
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	13
α-helix	137-143	7
β-strand	150-155	6	15
β-strand	160-166	7	15
β-strand	169-170	2	15
α-helix	172-174	3
β-strand	176-178	3	15
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	16
β-strand	247-250	4	16
α-helix	252-255	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-282	9
α-helix	290-295	6
β-strand	297-299	3	15
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	15
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-353	4
β-strand	357-358	2	13
α-helix	359-365	7
α-helix	367-369	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, E	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Twinfilin-1	B	protein	350	Homo sapiens	Q12792 (AlphaFold model)
F-actin-capping protein subunit alpha	C	protein	286	Mus musculus	P47753 (AlphaFold model)
F-actin-capping protein subunit beta	D	protein	272	Mus musculus	Q923G3 (AlphaFold model)

Sequence of entity 1 (A, E), FASTA

>7CCC_1 Actin, alpha skeletal muscle (chains A, E)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (B), FASTA

>7CCC_2 Twinfilin-1 (chains B)
MSHQTGIQASEDVKEIFARARNGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPL
LEDKQPCYILFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDE
VFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVGVDTKHQTLQGVAF
PISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNTELKDLPKRIPKDSARYHFFL
YKHSHEGDYLESIVFIYSMPGYTCSIRERMLYSSCKSRLLEIVERQLQMDVIRKIEIDNG
DELTADFLYEEVHPKQHAHKQSFAKPKGPAGKRGIRRLIRGPAETEATTD

Sequence of entity 3 (C), FASTA

>7CCC_3 F-actin-capping protein subunit alpha (chains C)
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYDDQVLITEHGDLGNSRFLDPRNQISFKFDHLRKEASDPQPEDVDGGLKSW
RESCDSALRAYVKDHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPSAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSVTVSNEVQTTKEFIKIIESAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

Sequence of entity 4 (D), FASTA

>7CCC_4 F-actin-capping protein subunit beta (chains D)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KSGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLRSVQTFADKSKQEALKNDLVEALKRKQQC

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2

Primary citation

The structure of the actin filament uncapping complex mediated by twinfilin. Mwangangi, D.M., Manser, E., Robinson, R.C. Sci Adv (2021) 7. DOI 10.1126/sciadv.abd5271 · 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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