3AAE: Actin capping protein

Crystal structure of Actin capping protein in complex with CARMIL fragment. Determined by X-ray diffraction at 3.3 Å resolution. Released 17 Nov 2010.

Method: X-ray diffraction
Resolution: 3.3 Å
Organisms: Gallus gallus, Mus musculus
Chains: 15
Atoms: 22,177
Mol. weight: 342.86 kDa
Released: 17 Nov 2010

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

Secondary structure: helices and β-sheets

3AAE contains 128 α-helices and 105 β-strands across 15 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.

Chains A, G and I: 10 helices, 11 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	63-65	3	1
β-strand	74-76	3	1
β-strand	81	1	2
β-strand	86-89	4	2
β-strand	94-99	6	2
β-strand	104-110	7	2
α-helix	118-135	18
β-strand	139-148	10	3
β-strand	151-164	14	3
α-helix	165-167	3
β-strand	169-182	14	3
β-strand	185-198	14	3
β-strand	202-217	16	3
α-helix	221-249	29
α-helix	250-255	6
α-helix	271-275	5

Chain B: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
α-helix	46-47	2
β-strand	48-52	5	4
β-strand	57-61	5	4
α-helix	63-65	3
β-strand	66-67	2	5
β-strand	70-72	3	5
β-strand	79-80	2	5
α-helix	91-112	22
β-strand	116-123	8	3
β-strand	127-137	11	3
β-strand	145-158	14	3
β-strand	164-179	16	3
α-helix	182-184	3
β-strand	186-202	17	3
α-helix	209-230	22
α-helix	231-235	5
α-helix	236-241	6
α-helix	248-250	3
α-helix	251-263	13

Chains C and E: 10 helices, 11 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	63-65	3	6
β-strand	74-76	3	6
β-strand	81	1	7
β-strand	86-89	4	7
β-strand	94-99	6	7
β-strand	104-110	7	7
α-helix	118-135	18
β-strand	139-148	10	8
β-strand	151-164	14	8
α-helix	165-167	3
β-strand	169-182	14	8
β-strand	185-198	14	8
β-strand	202-217	16	8
α-helix	221-249	29
α-helix	250-255	6
α-helix	271-274	4

Chain D: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
α-helix	46-47	2
β-strand	48-52	5	9
β-strand	57-61	5	9
α-helix	63-65	3
β-strand	66-67	2	10
β-strand	70-72	3	10
β-strand	79-80	2	10
α-helix	91-112	22
β-strand	116-123	8	8
β-strand	127-137	11	8
β-strand	145-158	14	8
β-strand	164-179	16	8
α-helix	182-184	3
β-strand	186-202	17	8
α-helix	209-230	22
α-helix	231-235	5
α-helix	236-241	6
α-helix	252-256	5
α-helix	261-264	4

Chain F: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
α-helix	46-47	2
β-strand	48-52	5	14
β-strand	57-61	5	14
α-helix	63-65	3
β-strand	66-67	2	15
β-strand	70-72	3	15
β-strand	79-80	2	15
α-helix	91-112	22
β-strand	116-123	8	13
β-strand	127-137	11	13
β-strand	145-158	14	13
β-strand	164-179	16	13
α-helix	182-184	3
β-strand	186-202	17	13
α-helix	209-229	21
α-helix	230-235	6
α-helix	236-241	6

Chain H: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	4-13	10
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
α-helix	46-47	2
β-strand	48-52	5	19
β-strand	57-61	5	19
α-helix	63-65	3
β-strand	66-67	2	20
β-strand	70-72	3	20
β-strand	79-80	2	20
α-helix	91-112	22
β-strand	116-123	8	18
β-strand	127-137	11	18
β-strand	145-158	14	18
β-strand	164-179	16	18
α-helix	182-184	3
β-strand	186-202	17	18
α-helix	209-230	22
α-helix	231-235	5
α-helix	236-241	6
α-helix	248-250	3

Chain J: 13 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	5-13	9
α-helix	18-20	3
α-helix	21-31	11
α-helix	33-35	3
α-helix	36-42	7
α-helix	46-47	2
β-strand	48-52	5	24
β-strand	57-61	5	24
α-helix	63-65	3
β-strand	66-67	2	25
β-strand	70-72	3	25
β-strand	79-80	2	25
α-helix	91-112	22
β-strand	116-123	8	23
β-strand	127-137	11	23
β-strand	145-158	14	23
β-strand	164-179	16	23
α-helix	182-184	3
β-strand	186-202	17	23
α-helix	209-230	22
α-helix	231-235	5
α-helix	236-243	8
α-helix	248-250	3

Chains V and W: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	989-992	4
α-helix	994-995	2

3 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
F-actin-capping protein subunit alpha-1	A, C, E, G, I	protein	286	Gallus gallus	P13127 (AlphaFold model)
F-actin-capping protein subunit beta isoforms 1 and 2	B, D, F, H, J	protein	277	Gallus gallus	P14315 (AlphaFold model)
32mer peptide from Leucine-rich repeat-containing protein 16A	V, W, X, Y, Z	protein	37	Mus musculus	Q6EDY6 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, I), FASTA

>3AAE_1 F-actin-capping protein subunit alpha-1 (chains A, C, E, G, I)
MADFEDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQW
RDACDSALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

Sequence of entity 2 (B, D, F, H, J), FASTA

>3AAE_2 F-actin-capping protein subunit beta isoforms 1 and 2 (chains B, D, F, H, J)
MSDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYL
LCDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVY
LWDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTN
KTGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIV
NGLRSIDAIPDNQKYKQLQRELSQVLTQRQIYIQPDN

Sequence of entity 3 (V, W, X, Y, Z), FASTA

>3AAE_3 32mer peptide from Leucine-rich repeat-containing protein 16A (chains V, W, X, Y, Z)
GPLGSSSGLISELPSEEGRRLEHFTKLRPKRNKKQQP

Primary citation

Two distinct mechanisms for the regulation of actin capping protein-competitive or allosteric inhibitions. Takeda, S., Minakata, S., Narita, A. et al. To be published.

Other PDB entries of the same protein (UniProt P13127 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7DS6 1.69 Å, Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera…
3AA0 1.7 Å, Crystal structure of Actin Capping Protein in complex with the Cp-binding motif derived…
7DS4 1.85 Å, Crystal structure of actin capping protein in complex with twinflin-1 C-terminus tail…
3AA1 1.9 Å, Crystal structure of Actin capping protein in complex with the Cp-binding motif derived…
3AA6 1.9 Å, Crystal structure of Actin capping protein in complex with the Cp-binding motif derived…
3AA7 1.9 Å, Crystal structure of Actin capping protein
7DS2 1.95 Å, Crystal structure of actin capping protein in complex with twinflin-1 C-terminus tail
7DS8 1.95 Å, Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera…
3LK4 1.99 Å, Crystal structure of CapZ bound to the uncapping motif from CD2AP
9BLI 2.0 Å, Crystal structure of Actin capping protein in complex with a fragment of Legionella…
7DS3 2.09 Å, Crystal structure of actin capping protein in complex with twinflin-2 C-terminus tail
1IZN 2.1 Å, Crystal Structure of Actin Filament Capping Protein CapZ

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