8RV2: Formin INF2

Structure of the formin INF2 bound to the barbed end of F-actin. Determined by electron microscopy at 3.41 Å resolution. Released 10 Apr 2024.

Method: Electron microscopy
Resolution: 3.41 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 6
Atoms: 17,248
Mol. weight: 338.39 kDa
Ligands: ADP, MG, PO4, ATP
Released: 10 Apr 2024

Explore 8RV2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8RV2 contains 138 α-helices and 93 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.

Chain A: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	1
β-strand	17-21	5	1
β-strand	29-31	3	1
β-strand	35-38	4	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	88-93	6
β-strand	103-107	5	1
α-helix	113-122	10
α-helix	123-127	5
β-strand	132-136	5	1
α-helix	137-145	9
β-strand	151-155	5	4
β-strand	160-163	4	4
β-strand	165-166	2	5
β-strand	169-170	2	5
α-helix	172-174	3
β-strand	176-178	3	4
α-helix	183-193	11
α-helix	194-196	3
α-helix	203-215	13
α-helix	223-232	10
α-helix	234-236	3
β-strand	238-241	4	6
β-strand	247-250	4	6
α-helix	253-256	4
α-helix	257-261	5
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	309-318	10
β-strand	329-330	2	4
α-helix	335-337	3
α-helix	338-346	9
α-helix	351-354	4
α-helix	359-362	4
α-helix	366-368	3
α-helix	369-373	5

Chain B: 26 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	6-7	2
β-strand	8-12	5	7
β-strand	16-21	6	7
β-strand	22	1	8
β-strand	24	1	8
β-strand	29-32	4	7
β-strand	35-38	4	9
β-strand	53-54	2	9
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	9
β-strand	71-72	2	10
β-strand	75-76	2	10
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	7
α-helix	113-122	10
α-helix	123-127	5
β-strand	131-136	6	7
α-helix	137-145	9
β-strand	150-155	6	11
β-strand	160-166	7	11
β-strand	169-170	2	11
α-helix	172-174	3
β-strand	176-178	3	11
α-helix	182-193	12
α-helix	204-216	13
α-helix	223-232	10
β-strand	238-241	4	12
β-strand	247-250	4	12
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	290-295	6
β-strand	297-300	4	11
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	11
α-helix	338-348	11
α-helix	352-354	3
β-strand	357-358	2	7
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain C: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	13
β-strand	16-21	6	13
β-strand	29-32	4	13
β-strand	35-38	4	14
β-strand	41	1	5
β-strand	53-54	2	14
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	14
β-strand	71-72	2	15
β-strand	75-76	2	15
α-helix	79-87	9
α-helix	88-93	6
α-helix	98-100	3
β-strand	103-107	5	13
α-helix	113-125	13
β-strand	131-136	6	13
α-helix	137-144	8
β-strand	150-155	6	16
β-strand	160-166	7	16
β-strand	169-170	2	16
β-strand	176-178	3	16
α-helix	182-193	12
α-helix	203-216	14
α-helix	223-232	10
α-helix	234-236	3
β-strand	238-241	4	17
β-strand	247-250	4	17
α-helix	253-256	4
α-helix	258-261	4
α-helix	264-267	4
α-helix	274-283	10
α-helix	290-293	4
β-strand	297-300	4	16
α-helix	302-305	4
α-helix	309-320	12
β-strand	329-330	2	16
α-helix	335-337	3
α-helix	338-348	11
α-helix	350-352	3
β-strand	357-358	2	13
α-helix	359-365	7
α-helix	366-371	6

Chain D: 23 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	8-10	3	18
β-strand	11-12	2	19
β-strand	16-19	4	19
β-strand	21	1	18
β-strand	29-32	4	19
β-strand	35-36	2	20
β-strand	37-38	2	21
β-strand	42	1	11
β-strand	53-54	2	20
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-66	2	21
β-strand	71-72	2	22
β-strand	75-76	2	22
α-helix	79-88	10
α-helix	89-93	5
β-strand	103-107	5	18
α-helix	113-121	9
α-helix	122-127	6
β-strand	132-136	5	18
α-helix	137-143	7
β-strand	150-154	5	23
β-strand	155	1	24
β-strand	160-162	3	24
β-strand	163-166	4	23
β-strand	169-170	2	23
α-helix	172-174	3
β-strand	176-178	3	24
α-helix	182-193	12
α-helix	204-216	13
α-helix	223-232	10
α-helix	234-236	3
β-strand	238-241	4	25
β-strand	247-250	4	25
α-helix	253-256	4
α-helix	258-261	4
α-helix	274-282	9
α-helix	287-294	8
β-strand	297-300	4	23
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	23
α-helix	335-337	3
α-helix	338-347	10
α-helix	350-355	6
β-strand	357	1	18
α-helix	359-362	4
α-helix	367-370	4

Chain E: 21 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	565-568	4
β-strand	571	1	26
α-helix	572-573	2
α-helix	583-587	5
α-helix	599-604	6
α-helix	635-644	10
α-helix	652-655	4
α-helix	657-661	5
α-helix	669-677	9
α-helix	682-690	9
α-helix	700-710	11
α-helix	714-750	37
α-helix	753-768	16
β-strand	780	1	27
α-helix	782-787	6
β-strand	792	1	28
β-strand	799	1	28
α-helix	800-808	9
α-helix	818-821	4
α-helix	823-828	6
α-helix	833-856	24
α-helix	859-861	3
α-helix	862-866	5
α-helix	867-896	30
α-helix	907-932	26

Chain F: 20 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	565-568	4
β-strand	571	1	27
α-helix	572-573	2
α-helix	584-587	4
α-helix	599-605	7
α-helix	635-645	11
α-helix	652-661	10
α-helix	669-677	9
α-helix	682-690	9
α-helix	700-710	11
α-helix	714-749	36
α-helix	753-768	16
β-strand	780	1	26
α-helix	782-790	9
β-strand	792	1	29
β-strand	799	1	29
α-helix	800-810	11
α-helix	818-821	4
α-helix	823-827	5
α-helix	833-855	23
α-helix	859-861	3
α-helix	862-866	5
α-helix	867-896	30
α-helix	907-932	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D	protein	375	Oryctolagus cuniculus	P68135 (AlphaFold model)
Isoform 2 of Inverted formin-2	E, F	protein	777	Homo sapiens	Q27J81 (AlphaFold model)

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

>8RV2_1 Actin, alpha skeletal muscle (chains A, B, C, D)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 2 (E, F), FASTA

>8RV2_2 Isoform 2 of Inverted formin-2 (chains E, F)
GGGGGMAPPAPPLPPPLPGSCEFLSPPPPPLPGLGCPPPPPPLLPGMGWGPPPPPPPLLP
CTCSPPVAGGMEEVIVAQVDHGLGSAWVPSHRRVNPPTLRMKKLNWQKLPSNVAREHNSM
WASLSSPDAEAVEPDFSSIERLFSFPAAKPKEPTMVAPRARKEPKEITFLDAKKSLNLNI
FLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLASADH
FYLLLLAIPCYQLRIECMLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILR
IGNFLNYGSHTGDADGFKISTLLKLTETKSQQNRVTLLHHVLEEAEKSHPDLLQLPRDLE
QPSQAAGINLEIIRSEASSNLKKLLETERKVSASVAEVQEQYTERLQASISAFRALDELF
EAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLFLRALKENKDRKEQAAKAERRKQQ
LAEEEARRPRGEDGKPVRKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTDGGSKAA
SMDPPRATEPVATSNPAGDPVGSTRCPASEPGLDATTASESRGWDLVDAVTPGPQPTLEQ
LEEGGPRPLERRSSWYVDASDVLTTEDPQCPQPLEGAWPVTLGDAQALKPLKFSSNQPPA
AGSSRQDAKDPTSLLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPES
ALDTSLDKSFSEDAVTDSSGSGTLPRARGRASKGTGKRRKKRPSRSQEGLRPRPKAK

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	3
MG	Magnesium ion	Mg	4
PO4	Phosphate ion	O4 P	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1

Primary citation

Molecular mechanism of actin filament elongation by formins. Oosterheert, W., Boiero Sanders, M., Funk, J. et al. Science (2024) 384:eadn9560-eadn9560. DOI 10.1126/science.adn9560 · 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

Browse structure collections

About this viewer

MolViewer shows 8RV2 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.