2A41: Actin, alpha skeletal muscle

Ternary complex of the WH2 Domain of WIP with Actin-DNAse I. Determined by X-ray diffraction at 2.6 Å resolution. Released 1 Nov 2005.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Oryctolagus cuniculus, Bos taurus
Chains: 3
Atoms: 5,498
Mol. weight: 75.69 kDa
Ligands: CA, MG, ATP
Released: 1 Nov 2005

Explore 2A41 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2A41 contains 40 α-helices and 41 β-strands across 3 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: 26 helices, 21 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	24	1	2
β-strand	29-32	4	1
β-strand	35-38	4	3
β-strand	42-44	3	4
β-strand	53-54	2	3
α-helix	56-60	5
α-helix	62-64	3
β-strand	65-68	4	3
β-strand	71-72	2	5
β-strand	75-76	2	5
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	6
β-strand	160-166	7	6
β-strand	169-170	2	6
α-helix	172-174	3
β-strand	176-178	3	6
α-helix	182-195	14
α-helix	203-216	14
α-helix	223-231	9
α-helix	234-236	3
β-strand	239-241	3	7
β-strand	247-249	3	7
α-helix	253-259	7
α-helix	264-267	4
α-helix	271-273	3
α-helix	274-282	9
α-helix	290-294	5
β-strand	297-300	4	6
α-helix	302-304	3
α-helix	309-320	12
β-strand	329-330	2	6
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	367-369	3
α-helix	370-373	4

Chain B: 13 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	2-11	10	4
α-helix	13-16	4
α-helix	19-29	11
β-strand	34-40	7	4
α-helix	46-55	10
β-strand	64-67	4	4
α-helix	68-70	3
β-strand	71	1	8
β-strand	78	1	8
β-strand	79-84	6	4
β-strand	90-96	7	9
α-helix	102-107	6
β-strand	114-119	6	9
β-strand	127-132	6	9
α-helix	137-139	3
α-helix	140-158	19
β-strand	163-168	6	9
α-helix	178-183	6
α-helix	185-188	4
β-strand	192-194	3	9
β-strand	203	1	10
β-strand	212-217	6	9
α-helix	219-222	4
β-strand	225	1	11
α-helix	226	1
β-strand	231-232	2	4
α-helix	235-239	5
α-helix	243-249	7
β-strand	252	1	10
β-strand	255-258	4	4
β-strand	259	1	11

Chain C: 1 helix, 2 β-strands

Element	Residues	Length	Sheet
α-helix	33-42	10
β-strand	47	1	2
β-strand	52-53	2	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A	protein	375	Oryctolagus cuniculus	P68135 (AlphaFold model)
Deoxyribonuclease-1	B	protein	260	Bos taurus	P00639 (AlphaFold model)
Wiskott-Aldrich syndrome protein interacting protein	C	protein	32		O43516 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2A41_1 Actin, alpha skeletal muscle (chains A)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 2 (B), FASTA

>2A41_2 Deoxyribonuclease-1 (chains B)
LKIAAFNIRTFGETKMSNATLASYIVRIVRRYDIVLIQEVRDSHLVAVGKLLDYLNQDDP
NTYHYVVSEPLGRNSYKERYLFLFRPNKVSVLDTYQYDDGCESCGNDSFSREPAVVKFSS
HSTKVKEFAIVALHSAPSDAVAEINSLYDVYLDVQQKWHLNDVMLMGDFNADCSYVTSSQ
WSSIRLRTSSTFQWLIPDSADTTATSTNCAYDRIVVAGSLLQSSVVPGSAAPFDFQAAYG
LSNEMALAISDHYPVEVTLT

Sequence of entity 3 (C), FASTA

>2A41_3 Wiskott-Aldrich syndrome protein interacting protein (chains C)
EQAGRNALLSDISKGKKLKKTVTNDRSAPILD

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	2
MG	Magnesium ion	Mg	1
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	1

Water and common crystallization additives (FMT) are not listed.

Primary citation

Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Chereau, D., Kerff, F., Graceffa, P. et al. Proc Natl Acad Sci U S A (2005) 102:16644-16649. DOI 10.1073/pnas.0507021102 · 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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