9EC0: CARMIL dimer

Structure of the CARMIL dimer bound to Capping Protein. Determined by electron microscopy at 3.4 Å resolution. Released 21 Jan 2026.

Method: Electron microscopy
Resolution: 3.4 Å
Organism: Homo sapiens
Chains: 6
Atoms: 23,388
Mol. weight: 365.8 kDa
Released: 21 Jan 2026

Explore 9EC0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9EC0 contains 140 α-helices and 94 β-strands across 6 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 and B: 51 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	8-9	2
α-helix	10-20	11
α-helix	25-26	2
β-strand	28-36	9	1
β-strand	40-48	9	1
β-strand	52-57	6	1
β-strand	64-69	6	1
α-helix	70-72	3
β-strand	73-78	6	1
β-strand	83-88	6	1
β-strand	92-96	5	1
α-helix	100-117	18
β-strand	130-132	3	1
α-helix	135-147	13
α-helix	149-150	2
α-helix	155-170	16
α-helix	172-174	3
α-helix	176-188	13
β-strand	193-195	3	2
α-helix	207-212	6
β-strand	222-226	5	2
α-helix	232-244	13
β-strand	250-254	5	2
α-helix	260-272	13
β-strand	280-282	3	2
α-helix	289-300	12
β-strand	309-311	3	2
α-helix	319-331	13
β-strand	341-343	3	2
α-helix	355-362	8
β-strand	369-371	3	2
β-strand	378	1	3
α-helix	379-389	11
β-strand	396-398	3	2
β-strand	403	1	3
α-helix	411-413	3
α-helix	414-421	8
β-strand	428-430	3	2
α-helix	438-449	12
β-strand	457-460	4	2
α-helix	467-476	10
β-strand	484-488	5	2
α-helix	495-497	3
α-helix	498-505	8
β-strand	513-515	3	2
α-helix	529-539	11
β-strand	548-550	3	2
α-helix	557-560	4
α-helix	561-565	5
β-strand	575-577	3	2
α-helix	585-595	11
β-strand	603-605	3	2
α-helix	613-622	10
β-strand	631	1	2
α-helix	636-642	7
α-helix	647-666	20
α-helix	672-679	8
α-helix	680-684	5
α-helix	685-704	20
α-helix	711-728	18
α-helix	733-736	4
α-helix	755-774	20
α-helix	779-789	11
α-helix	800-811	12
α-helix	815-820	6
α-helix	821-827	7
α-helix	828-869	42
α-helix	904-910	7
α-helix	919-923	5
α-helix	931-933	3
α-helix	972-975	4
α-helix	981-983	3
α-helix	990-991	2
α-helix	1001-1004	4
α-helix	1014-1019	6
α-helix	1026-1029	4
α-helix	1034-1036	3

Chains C and E: 11 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	43-61	19
β-strand	64-66	3	7
α-helix	67	1
β-strand	73-75	3	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	115-117	3
α-helix	118-135	18
β-strand	139-148	10	9
β-strand	151-164	14	9
β-strand	169-180	12	9
β-strand	185-198	14	9
β-strand	204-217	14	9
α-helix	221-249	29
α-helix	250-254	5
α-helix	255-258	4
α-helix	272-276	5

Chains D and F: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	3-12	10
α-helix	21-31	11
α-helix	36-42	7
α-helix	45-47	3
β-strand	49-51	3	10
β-strand	58-60	3	10
β-strand	66-67	2	11
β-strand	70-72	3	11
β-strand	79-80	2	11
α-helix	91-111	21
β-strand	116-123	8	9
β-strand	127-137	11	9
β-strand	144-158	15	9
β-strand	164-181	18	9
β-strand	185-202	18	9
α-helix	209-230	22
α-helix	231-235	5
α-helix	236-243	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
F-actin-uncapping protein LRRC16A	A, B	protein	1062	Homo sapiens	Q5VZK9 (AlphaFold model)
F-actin-capping protein subunit alpha-1	C, E	protein	286	Homo sapiens	P52907 (AlphaFold model)
F-actin-capping protein subunit beta	D, F	protein	276	Homo sapiens	P47756 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9EC0_1 F-actin-uncapping protein LRRC16A (chains A, B)
MHHHHHHGMTEESSDVPRELIESIKDVIGRKIKISVKKKVKLEVKGDKVENKVLVLTSCR
AFLVTARIPTKLELTFSYLEIHGVVCSKSAQMIVETEKCSISMKMASPEDVSEVLAHIGT
CLRKIFPGLSPVRIMKKVSMEPSERLASLQALWDSQTVAEQGPCGGFSQMYACVCDWLGF
SYREEVQWDVDTIYLTQDTRELNLQDFSHLDHRDLIPIIAALEYNQWFTKLSSKDLKLST
DVCEQILRVVSRSNRLEELVLENAGLRTDFAQKLASALAHNPNSGLHTINLAGNPLEDRG
VSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPLTASTLVHLDLSGNVLRGD
DLSHMYNFLAQPNAIVHLDLSNTECSLDMVCGALLRGCLQYLAVLNLSRTVFSHRKGKEV
PPSFKQFFSSSLALMHINLSGTKLSPEPLKALLLGLACNHNLKGVSLDLSNCELRSGGAQ
VLEGCIAEIHNITSLDISDNGLESDLSTLIVWLSKNRSIQHLALGKNFNNMKSKNLTPVL
DNLVQMIQDEESPLQSLSLADSKLKTEVTIIINALGSNTSLTKVDISGNGMGDMGAKMLA
KALQINTKLRTVIWDKNNITAQGFQDIAVAMEKNYTLRFMPIPMYDASQALKTNPEKTED
ALQKIENYLLRNHETRKYLQEQAYRLQQGIVTSTTQQMIDRICVKVQDHLNSLRNCGGDA
IQEDLKSAERLMRDAKNSKTLLPNLYHVGGASWAGASGLLSSPIQETLESMAGEVTRVVD
EQLKALLESMVDAAENLCPNVMKKAHIRQDLIHASTEKISIPRTFVKNVLLEQSGIDILN
KISEVKLTVASFLSDRIVDEILDALSHCHHKLADHFSRRGKTLPQQESLEIELAEEKPVK
RSIITVEELTEIERLEDLDTCMMTPKSKRKSIHSRMLRPVSRAFEMEFDLDKALEEVPIH
IEDPPFPSLRQEKRSSGFISELPSEEGKKLEHFTKLRPKRNKKQQPTQAAVCAANIVSQD
GEQNGLMGRVDEGVDEFFTKKVTKMDSKKWSTRGWSHPQFEK

Sequence of entity 2 (C, E), FASTA

>9EC0_2 F-actin-capping protein subunit alpha-1 (chains C, E)
MADFDDRVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMD
QFTPVKIEGYEDQVLITEHGDLGNSRFLDPRNKISFKFDHLRKEASDPQPEEADGGLKSW
RESCDSALRAYVKDHYSNGFCTVYAKTIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFT
ITPPTAQVVGVLKIQVHYYEDGNVQLVSHKDVQDSLTVSNEAQTAKEFIKIIENAENEYQ
TAISENYQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGKEMQNA

Sequence of entity 3 (D, F), FASTA

>9EC0_3 F-actin-capping protein subunit beta (chains D, F)
SDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLL
CDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYL
WDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNK
SGSGTMNLGGSLTRQMEKDETVSDCSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVN
GLRSIDAIPDNQKFKQLQRELSQVLTQRQIYIQPDN

Primary citation

Structural basis for regulation of Capping Protein by the CARMIL dimer. Barrie, K.R., Dominguez, R. To be published.

Other PDB entries of the same protein (UniProt Q5VZK9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3LK2 2.2 Å, Crystal structure of CapZ bound to the uncapping motif from CARMIL
3LK3 2.68 Å, Crystal structure of CapZ bound to the CPI and CSI uncapping motifs from CARMIL

Browse structure collections

About this viewer

MolViewer shows 9EC0 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.