9QFB: Actin, cytoplasmic 1, N-terminally processed

Cryo-EM structure of the fully Coronin-1B-decorated actin filament in the ADP state. Determined by electron microscopy at 2.74 Å resolution. Released 8 Oct 2025.

Method: Electron microscopy
Resolution: 2.74 Å
Organism: Homo sapiens
Chains: 14
Atoms: 41,846
Mol. weight: 818.1 kDa
Ligands: MG, ADP
Released: 8 Oct 2025

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

Secondary structure: helices and β-sheets

9QFB contains 216 α-helices and 393 β-strands across 14 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: 22 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	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	137-144	8
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	182-194	13
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-262	10
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	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	368-371	4

Chain B: 22 helices, 19 β-strands

Element	Residues	Length	Sheet
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
β-strand	103-107	5	6
α-helix	113-125	13
β-strand	131-136	6	6
α-helix	137-144	8
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	182-194	13
α-helix	203-216	14
α-helix	223-230	8
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	9
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	9
α-helix	335-337	3
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	368-371	4

Chain C: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
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	41-42	2	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	113-121	9
α-helix	122-126	5
β-strand	131-136	6	11
α-helix	137-144	8
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	182-194	13
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	15
β-strand	247-250	4	15
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	14
α-helix	303-305	3
α-helix	309-320	12
β-strand	329-330	2	14
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	368-371	4

Chain D: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
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
β-strand	103-107	5	16
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	16
α-helix	137-144	8
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	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	20
β-strand	247-250	4	20
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-289	3
α-helix	290-294	5
β-strand	297-300	4	19
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	368-371	4

Chain E: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	21
β-strand	16-21	6	21
β-strand	29-32	4	21
β-strand	35-38	4	22
β-strand	42	1	14
β-strand	53-54	2	22
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	22
β-strand	71-72	2	23
β-strand	75-76	2	23
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	21
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	21
α-helix	137-144	8
β-strand	150-155	6	24
β-strand	160-166	7	24
β-strand	169-170	2	24
α-helix	172-174	3
β-strand	176-178	3	24
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	25
β-strand	247-250	4	25
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	24
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	24
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	21
α-helix	359-365	7
α-helix	368-371	4

Chain F: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	26
β-strand	16-21	6	26
β-strand	29-32	4	26
β-strand	35-38	4	27
β-strand	42	1	19
β-strand	53-54	2	27
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	27
β-strand	71-72	2	28
β-strand	75-76	2	28
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	26
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	26
α-helix	137-144	8
β-strand	150-155	6	29
β-strand	160-166	7	29
β-strand	169-170	2	29
α-helix	172-174	3
β-strand	176-178	3	29
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	30
β-strand	247-250	4	30
α-helix	253-262	10
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	29
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	29
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-355	6
β-strand	357-358	2	26
α-helix	359-365	7
α-helix	368-371	4

Chain G: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	31
β-strand	16-21	6	31
β-strand	29-32	4	31
β-strand	35-38	4	32
β-strand	42	1	24
β-strand	53-54	2	32
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	32
β-strand	71-72	2	33
β-strand	75-76	2	33
α-helix	79-87	9
α-helix	88-93	6
β-strand	103-107	5	31
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	31
α-helix	137-144	8
β-strand	150-155	6	34
β-strand	160-166	7	34
β-strand	169-170	2	34
α-helix	172-174	3
β-strand	176-178	3	34
α-helix	182-193	12
α-helix	194-196	3
α-helix	203-216	14
α-helix	223-231	9
β-strand	238-241	4	35
β-strand	247-250	4	35
α-helix	253-262	10
α-helix	264-267	4
α-helix	274-283	10
α-helix	287-294	8
β-strand	297-300	4	34
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	34
α-helix	335-337	3
α-helix	338-348	11
α-helix	353-355	3
β-strand	357-358	2	31
α-helix	359-365	7
α-helix	368-371	4

Chain H: 8 helices, 39 β-strands

Element	Residues	Length	Sheet
β-strand	16-19	4	36
α-helix	20-21	2
α-helix	22-24	3
β-strand	26-27	2	36
β-strand	31	1	37
β-strand	41-43	3	37
β-strand	47-52	6	37
β-strand	58-64	7	37
β-strand	69-70	2	36
α-helix	71-72	2
β-strand	78-81	4	37
β-strand	85-91	7	38
β-strand	94-102	9	38
β-strand	107-111	5	38
β-strand	121	1	37
β-strand	126-128	3	38
β-strand	135-140	6	39
β-strand	144	1	40
β-strand	147-152	6	39
β-strand	157-161	5	39
β-strand	166-171	6	39
β-strand	179-184	6	41
β-strand	191-195	5	41
β-strand	199-204	6	41
β-strand	209-215	7	41
β-strand	225-228	4	42
β-strand	234-238	5	42
β-strand	245-250	6	42
β-strand	251	1	43
β-strand	254	1	43
β-strand	260-265	6	42
β-strand	271-276	6	44
β-strand	281-286	6	44
β-strand	291-296	6	44
β-strand	305-311	7	44
β-strand	318	1	36
β-strand	321	1	36
α-helix	324-326	3
α-helix	329-331	3
β-strand	333-340	8	36
β-strand	344-351	8	36
β-strand	367-368	2	45
β-strand	374	1	40
α-helix	376-381	6
α-helix	386-388	3
β-strand	389-390	2	45
α-helix	393-395	3

6 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
Actin, cytoplasmic 1, N-terminally processed	A, B, C, D, E, F, G	protein	374	Homo sapiens	P60709 (AlphaFold model)
Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase	H, I, J, K, L, M, N	protein	688	Homo sapiens	P16455 (AlphaFold model), Q9BR76 (AlphaFold model)

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

>9QFB_1 Actin, cytoplasmic 1, N-terminally processed (chains A, B, C, D, E, F, G)
DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSK
RGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQ
IMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLA
GRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYE
LPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTFNSIMKCDVDIRKDLYANTVLSG
GTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQE
YDESGPSIVHRKCF

Sequence of entity 2 (H, I, J, K, L, M, N), FASTA

>9QFB_2 Coronin-1B,Methylated-DNA--protein-cysteine methyltransferase (chains H, I, J, K, L, M, N)
GAMGSMSFRKVVRQSKFRHVFGQPVKNDQCYEDIRVSRVTWDSTFCAVNPKFLAVIVEAS
GGGAFLVLPLSKTGRIDKAYPTVCGHTGPVLDIDWCPHNDEVIASGSEDCTVMVWQIPEN
GLTSPLTEPVVVLEGHTKRVGIIAWHPTARNVLLSAGCDNVVLIWNVGTAEELYRLDSLH
PDLIYNVSWNHNGSLFCSACKDKSVRIIDPRRGTLVAEREKAHEGARPMRAIFLADGKVF
TTGFSRMSERQLALWDPENLEEPMALQELDSSNGALLPFYDPDTSVVYVCGKGDSSIRYF
EITEEPPYIHFLNTFTSKEPQRGMGSMPKRGLEVSKCEIARFYKLHERKCEPIVMTVPRK
SDLFQDDLYPDTAGPEAALEAEEWVSGRDADPILISLREAYVPSKQRDLKISRRNVLSDS
RPAMAPGSSHLGAPASTTTAADATPSGSLARAGEAGKLEEVMQELRALRALVKEQGDRIC
RLEEQLGRMENGDAGTGGGGSGGGGSMDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLL
GKGTSAADAVEVPAPAAVLGGPEPLMQATAWLNAYFHQPEAIEEFPVPALHHPVFQQESF
TRQVLWKLLKVVKFGEVISYQQLAALAGNPAATAAVKTALSGNPVPILIPCHRVVSSSGA
VGGYEGGLAVKEWLLAHEGHRLGKPGLG

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	7
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	7

Primary citation

Choreography of rapid actin filament disassembly by coronin, cofilin, and AIP1. Oosterheert, W., Boiero Sanders, M., Hofnagel, O. et al. Cell (2025) 188:6845. DOI 10.1016/j.cell.2025.09.016 · PubMed

Other PDB entries of the same protein (UniProt P60709 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6MBK 1.69 Å, SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, First…
6OX0 1.75 Å, SETD3 in Complex with an Actin Peptide with Sinefungin Replacing SAH as Cofactor
6MBJ 1.78 Å, SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, P21…
6OX3 1.78 Å, SETD3 in Complex with an Actin Peptide with His73 Replaced with Lysine
7W28 1.79 Å, Crystal Structure of SETD3-SAH in complex with betaA-4PyrAla73 peptide
6OX1 1.95 Å, SETD3 in Complex with an Actin Peptide with Target Histidine Partially Methylated
6ICT 1.95 Å, Structure of SETD3 bound to SAH and methylated actin
6OX2 2.09 Å, SETD3in Complex with an Actin Peptide with the Target Histidine Fully Methylated
6OX5 2.1 Å, A SETD3 Mutant (N255A) in Complex with an Actin Peptide with His73 Replaced with Lysine
6ICV 2.15 Å, Structure of SETD3 bound to SAH and unmodified actin
9QEW 2.18 Å, Cryo-EM structure of the undecorated actin filament in the ADP-Pi state.
6MBL 2.2 Å, SETD3, a Histidine Methyltransferase, in Complex with an Actin Peptide and SAH, Second…

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