9B03: INF2 in the Middle of F-Actin

INF2 in the Middle of F-Actin (Up state). Determined by electron microscopy at 2.95 Å resolution. Released 29 May 2024.

Method: Electron microscopy
Resolution: 2.95 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 8
Atoms: 23,896
Mol. weight: 350.49 kDa
Ligands: ADP, MG
Released: 29 May 2024

Explore 9B03 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9B03 contains 193 α-helices and 134 β-strands across 8 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: 23 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
α-helix	41-42	2
β-strand	53-54	2	2
α-helix	56-60	5
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	88-94	7
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	182-193	12
α-helix	204-216	13
α-helix	223-232	10
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	287-289	3
α-helix	290-294	5
β-strand	297-300	4	4
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	4
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-368	3
α-helix	370-373	4

Chain B: 23 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	6
β-strand	16-20	5	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	79-88	10
α-helix	89-94	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	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	182-193	12
α-helix	204-215	12
α-helix	223-232	10
β-strand	238-241	4	10
β-strand	247-250	4	10
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-283	10
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	338-347	10
α-helix	350-352	3
β-strand	357-358	2	6
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain C: 23 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	103-105	3	11
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-134	4	11
α-helix	137-145	9
β-strand	150-155	6	14
β-strand	160-166	7	14
β-strand	169-170	2	14
β-strand	176-178	3	14
α-helix	182-193	12
α-helix	204-216	13
α-helix	223-232	10
β-strand	238-241	4	15
β-strand	247-250	4	15
α-helix	253-256	4
α-helix	258-260	3
α-helix	264-267	4
α-helix	274-283	10
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	338-347	10
α-helix	350-354	5
β-strand	357-358	2	11
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

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	41-42	2	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	88-94	7
α-helix	98-100	3
β-strand	103-107	5	16
α-helix	113-125	13
β-strand	131-136	6	16
α-helix	137-145	9
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	182-192	11
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	258-260	3
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	303-305	3
α-helix	309-320	12
β-strand	329-330	2	19
α-helix	338-347	10
α-helix	351-354	4
β-strand	357-358	2	16
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain E: 24 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	41-42	2	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
α-helix	98-100	3
β-strand	103-107	5	21
α-helix	113-125	13
β-strand	131-136	6	21
α-helix	137-145	9
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	182-193	12
α-helix	203-215	13
α-helix	223-232	10
β-strand	238-241	4	25
β-strand	247-250	4	25
α-helix	253-256	4
α-helix	258-260	3
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	24
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	24
α-helix	338-346	9
α-helix	350-352	3
β-strand	357-358	2	21
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain F: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
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	41-42	2	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	88-94	7
α-helix	98-100	3
β-strand	103-107	5	26
α-helix	113-125	13
β-strand	131-136	6	26
α-helix	137-145	9
β-strand	150-155	6	29
β-strand	160-166	7	29
β-strand	169-170	2	29
β-strand	176-178	3	29
α-helix	182-192	11
α-helix	193-195	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	253-256	4
α-helix	259-262	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-294	5
β-strand	297-300	4	29
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	29
α-helix	338-347	10
α-helix	350-355	6
β-strand	357-358	2	26
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain G: 28 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	558-560	3
β-strand	564	1	31
α-helix	565-568	4
α-helix	570	1
β-strand	571	1	32
α-helix	572-573	2
α-helix	574-577	4
α-helix	583-588	6
α-helix	595-597	3
α-helix	599-605	7
β-strand	607	1	31
α-helix	608-610	3
β-strand	630	1	33
α-helix	635-644	10
α-helix	652-660	9
α-helix	669-677	9
α-helix	679-681	3
α-helix	682-690	9
β-strand	698	1	33
α-helix	700-709	10
α-helix	714-749	36
α-helix	753-768	16
β-strand	780	1	34
α-helix	782-784	3
α-helix	786-789	4
β-strand	792	1	35
β-strand	799	1	35
α-helix	800-810	11
α-helix	813-817	5
α-helix	818-821	4
α-helix	823-828	6
α-helix	833-855	23
α-helix	859-896	38
α-helix	906-946	41
α-helix	972-979	8
α-helix	980-982	3

Chain H: 24 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	558-560	3
β-strand	564	1	36
β-strand	571	1	34
α-helix	572-573	2
α-helix	574-577	4
α-helix	583-588	6
α-helix	595-597	3
α-helix	599-605	7
β-strand	607	1	36
α-helix	608-609	2
β-strand	630	1	37
α-helix	635-646	12
α-helix	652-661	10
α-helix	669-677	9
α-helix	682-689	8
α-helix	695-697	3
β-strand	698	1	37
α-helix	700-709	10
α-helix	714-749	36
α-helix	753-768	16
β-strand	780	1	32
α-helix	782-787	6
β-strand	792	1	38
β-strand	799	1	38
α-helix	800-810	11
α-helix	813-817	5
α-helix	818-821	4
α-helix	823-827	5
α-helix	833-855	23
α-helix	859-896	38
α-helix	906-946	41
α-helix	972-978	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D, E, F	protein	371	Oryctolagus cuniculus	P68135 (AlphaFold model)
Inverted formin-2	G, H	protein	437	Homo sapiens	Q27J81 (AlphaFold model)

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

>9B03_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F)
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGI
LTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMF
ETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRD
LTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPD
GQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDE
AGPSIVHRKCF

Sequence of entity 2 (G, H), FASTA

>9B03_2 Inverted formin-2 (chains G, H)
VPSHRRVNPPTLRMKKLNWQKLPSNVAREHNSMWASLSSPDAEAVEPDFSSIERLFSFPA
AKPKEPTMVAPRARKEPKEITFLDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVE
VLKQLLKLLPEKHEIENLRAFTEERAKLASADHFYLLLLAIPCYQLRIECMLLCEGAAAV
LDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTE
TKSQQNRVTLLHHVLEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEASSNLKKLLET
ERKVSASVAEVQEQYTERLQASISAFRALDELFEAIEQKQRELADYLCEDAQQLSLEDTF
STMKAFRDLFLRALKENKDRKEQAAKAERRKQQLAEEEARRPRGEDGKPVRKGPGKQEEV
CVIDALLADIRKGFQLR

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6
MG	Magnesium ion	Mg	6

Primary citation

Mechanisms of actin filament severing and elongation by formins. Palmer, N.J., Barrie, K.R., Dominguez, R. Nature (2024) 632:437-442. DOI 10.1038/s41586-024-07637-0 · 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

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