9QGK: F-actin decorated by ITPKA

F-actin decorated by ITPKA. Determined by electron microscopy at 2.97 Å resolution. Released 25 Mar 2026.

Method: Electron microscopy
Resolution: 2.97 Å
Organisms: Homo sapiens, Gallus, Amanita phalloides
Chains: 13
Atoms: 15,640
Mol. weight: 470.65 kDa
Ligands: ADP, MG
Released: 25 Mar 2026

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

Secondary structure: helices and β-sheets

9QGK contains 134 α-helices and 100 β-strands across 10 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 C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	31-48	18

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	31-45	15

Chains D and E: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	31-49	19

Chain F: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
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	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-125	13
β-strand	131-136	6	1
α-helix	137-145	9
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	223-231	9
β-strand	238-241	4	5
β-strand	247-250	4	5
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	4
α-helix	302-304	3
α-helix	309-320	12
α-helix	322	1
β-strand	329-330	2	4
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-371	5

Chain G: 25 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
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	42	1	8
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	9
β-strand	75-76	2	9
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	6
α-helix	113-125	13
β-strand	131-136	6	6
α-helix	137-145	9
β-strand	150-155	6	10
β-strand	160-166	7	10
β-strand	169-170	2	10
α-helix	172-174	3
β-strand	176-178	3	10
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	11
β-strand	247-250	4	11
α-helix	253-259	7
α-helix	264-267	4
α-helix	274-284	11
α-helix	287-294	8
β-strand	297-300	4	10
α-helix	302-305	4
α-helix	309-320	12
α-helix	322	1
β-strand	329-330	2	10
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	367-371	5

Chain H: 27 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	12
β-strand	16-21	6	12
β-strand	29-32	4	12
β-strand	35-38	4	13
α-helix	41	1
β-strand	42	1	14
β-strand	53-54	2	13
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	13
β-strand	71-72	2	15
β-strand	75-76	2	15
α-helix	79-87	9
α-helix	88-94	7
α-helix	98-100	3
β-strand	103-107	5	12
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	12
α-helix	137-145	9
β-strand	150-155	6	8
β-strand	160-166	7	8
β-strand	169-170	2	8
α-helix	172-174	3
β-strand	176-178	3	8
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	16
β-strand	247-250	4	16
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	8
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	8
α-helix	335-337	3
α-helix	338-348	11
α-helix	351-355	5
β-strand	357-358	2	12
α-helix	359-363	5
α-helix	367-371	5

Chain I: 27 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	17
β-strand	16-21	6	17
β-strand	29-32	4	17
β-strand	35-38	4	18
β-strand	53-54	2	18
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	18
β-strand	71-72	2	19
β-strand	75-76	2	19
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	17
α-helix	113-125	13
β-strand	131-136	6	17
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	182-193	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	253-256	4
α-helix	258-261	4
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	14
α-helix	302-304	3
α-helix	309-320	12
α-helix	322	1
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	17
α-helix	359-365	7
α-helix	369-372	4

Chain J: 25 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	21
β-strand	16	1	22
β-strand	17-21	5	21
β-strand	29	1	21
β-strand	32	1	22
β-strand	35-38	4	23
β-strand	42	1	4
β-strand	53-54	2	23
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	23
β-strand	71-72	2	24
β-strand	75-76	2	24
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	21
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	21
α-helix	137-145	9
β-strand	150-155	6	25
β-strand	160-166	7	25
β-strand	169-170	2	25
α-helix	172-174	3
β-strand	176-178	3	25
α-helix	182-194	13
α-helix	203-216	14
α-helix	223-232	10
β-strand	238-241	4	26
β-strand	247-250	4	26
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	25
α-helix	302-305	4
α-helix	309-320	12
α-helix	322	1
β-strand	329-330	2	25
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-354	5
β-strand	357-358	2	21
α-helix	359-365	7
α-helix	367-371	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Inositol-trisphosphate 3-kinase A	A, B, C, D, E	protein	461	Homo sapiens	P23677 (AlphaFold model)
Actin, alpha skeletal muscle	F, G, H, I, J	protein	377	Gallus	P68139 (AlphaFold model)
Phalloidin	X, Y, Z	protein	7	Amanita phalloides

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

>9QGK_1 Inositol-trisphosphate 3-kinase A (chains A, B, C, D, E)
MTLPGGPTGMARPGGARPCSPGLERAPRRSVGELRLLFEARCAAVAAAAAAGEPRARGAK
RRGGQVPNGLPRAPPAPVIPQLTVTAEEPDVPPTSPGPPERERDCLPAAGSSHLQQPRRL
STSSVSSTGSSSLLEDSEDDLLSDSESRSRGNVQLEAGEDVGQKNHWQKIRTMVNLPVIS
PFKKRYAWVQLAGHTGSFKAAGTSGLILKRCSEPERYCLARLMADALRGCVPAFHGVVER
DGESYLQLQDLLDGFDGPCVLDCKMGVRTYLEEELTKARERPKLRKDMYKKMLAVDPEAP
TEEEHAQRAVTKPRYMQWREGISSSTTLGFRIEGIKKADGSCSTDFKTTRSREQVLRVFE
EFVQGDEEVLRRYLNRLQQIRDTLEVSEFFRRHEVIGSSLLFVHDHCHRAGVWLIDFGKT
TPLPDGQILDHRRPWEEGNREDGYLLGLDNLIGILASLAER

Sequence of entity 2 (F, G, H, I, J), FASTA

>9QGK_2 Actin, alpha skeletal muscle (chains F, G, H, I, J)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

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

>9QGK_3 Phalloidin (chains X, Y, Z)
PAWXATC

Ligands and cofactors

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

Primary citation

Evolutionarily conserved short linear motifs drive actin filament binding. Paraschiakos, T., Yuan, B., Hecht-Bucher, M. et al. Nat Cell Biol (2026) 28:1437-1452. DOI 10.1038/s41556-026-01979-9 · PubMed

Other PDB entries of the same protein (UniProt P23677 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8PP8 1.59 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PPE 1.59 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PPI 1.65 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PPH 1.7 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PP9 1.73 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PPA 1.73 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PPG 1.75 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PPJ 1.75 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PPD 1.77 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
1W2F 1.8 Å, Human Inositol (1,4,5)-trisphosphate 3-kinase substituted with selenomethionine
8PPB 1.8 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…
8PPF 1.85 Å, Human inositol 1,4,5-trisphosphate 3-kinase A (IP3K) catalytic domain in complex with…

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