6UBY: Isolated cofilin

Isolated cofilin bound to an actin filament. Determined by electron microscopy at 7.5 Å resolution. Released 1 Jan 2020.

Method: Electron microscopy
Resolution: 7.5 Å
Organisms: Oryctolagus cuniculus, Homo sapiens
Chains: 9
Atoms: 21,586
Mol. weight: 358.47 kDa
Ligands: MG, ADP
Released: 1 Jan 2020

Explore 6UBY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6UBY contains 161 α-helices and 156 β-strands across 9 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, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	1
β-strand	16	1	2
β-strand	17-21	5	1
β-strand	29	1	1
β-strand	32	1	2
β-strand	35-38	4	3
β-strand	46-48	3	4
β-strand	54	1	3
α-helix	56-60	5
β-strand	65-68	4	3
β-strand	71	1	5
β-strand	76	1	5
α-helix	80-91	12
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	6
β-strand	160-165	6	6
β-strand	170	1	6
α-helix	172-174	3
β-strand	176-178	3	6
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	7
β-strand	247-250	4	7
α-helix	253-256	4
α-helix	258-261	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	6
α-helix	302-305	4
α-helix	309-320	12
α-helix	338-347	10
α-helix	351-354	4
α-helix	356	1
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chains B, C, D, E and F: 22 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	8
β-strand	16	1	9
β-strand	17-21	5	8
β-strand	29	1	8
β-strand	32	1	9
β-strand	35-38	4	10
β-strand	54	1	10
α-helix	56-60	5
β-strand	65-68	4	10
β-strand	71	1	11
β-strand	76	1	11
α-helix	80-91	12
β-strand	103-107	5	8
α-helix	113-125	13
β-strand	131-136	6	8
α-helix	137-144	8
β-strand	150-155	6	12
β-strand	160-165	6	12
β-strand	170	1	12
α-helix	172-174	3
β-strand	176-178	3	12
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	13
β-strand	247-250	4	13
α-helix	253-256	4
α-helix	258-261	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	12
α-helix	302-305	4
α-helix	309-320	12
α-helix	338-347	10
α-helix	351-354	4
α-helix	356	1
β-strand	357-358	2	8
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain G: 12 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	150-155	6	38
β-strand	160-165	6	38
β-strand	170	1	38
α-helix	172-174	3
β-strand	176-178	3	38
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	39
β-strand	247-250	4	39
α-helix	253-256	4
α-helix	258-261	4
α-helix	272-273	2
α-helix	274-284	11
α-helix	290-294	5
β-strand	297-300	4	38
α-helix	302-305	4
α-helix	309-320	12

Chain H: 10 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	40
β-strand	16	1	41
β-strand	17-21	5	40
β-strand	29	1	40
β-strand	32	1	41
β-strand	35-38	4	42
β-strand	54	1	42
α-helix	56-60	5
β-strand	65-68	4	42
β-strand	71	1	43
β-strand	76	1	43
α-helix	80-91	12
β-strand	103-107	5	40
α-helix	113-125	13
β-strand	131-136	6	40
α-helix	137-144	8
α-helix	338-347	10
α-helix	351-354	4
α-helix	356	1
β-strand	357-358	2	40
α-helix	359-365	7
α-helix	366-368	3
α-helix	369-373	5

Chain I: 7 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	44
α-helix	9-19	11
α-helix	29-31	3
β-strand	33-36	4	45
β-strand	38	1	45
β-strand	39-40	2	44
β-strand	46-48	3	44
β-strand	54-56	3	45
β-strand	60	1	46
β-strand	64	1	46
α-helix	69-72	4
β-strand	81-87	7	45
β-strand	89-91	3	47
β-strand	95	1	47
β-strand	98-104	7	45
α-helix	111-119	9
α-helix	121-125	5
β-strand	133-137	5	45
α-helix	140-144	5
α-helix	147-153	7
β-strand	158-161	4	47
β-strand	164-165	2	47

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B, C, D, E, F, G, H	protein	377	Oryctolagus cuniculus	P68135 (AlphaFold model)
Cofilin-1	I	protein	166	Homo sapiens	P23528 (AlphaFold model)

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

>6UBY_1 Actin, alpha skeletal muscle (chains A, B, C, D, E, F, G, H)
MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEA
QSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREK
MTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRL
DLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEK
SYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNV
MSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWIT
KQEYDEAGPSIVHRKCF

Sequence of entity 2 (I), FASTA

>6UBY_2 Cofilin-1 (chains I)
MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDV
GQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS
KDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

Ligands and cofactors

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

Primary citation

Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments. Huehn, A.R., Bibeau, J.P., Schramm, A.C. et al. Proc Natl Acad Sci U S A (2020) 117:1478-1484. DOI 10.1073/pnas.1915987117 · 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

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