2VCP: N-Wasp VC domain

Crystal structure of N-Wasp VC domain in complex with skeletal actin. Determined by X-ray diffraction at 3.2 Å resolution. Released 4 Nov 2008.

Method: X-ray diffraction
Resolution: 3.2 Å
Organisms: ORYCTOLAGUS CUNICULUS, HOMO SAPIENS
Chains: 4
Atoms: 6,156
Mol. weight: 104.5 kDa
Ligands: ATP, CA
Released: 4 Nov 2008

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

Secondary structure: helices and β-sheets

2VCP contains 55 α-helices and 43 β-strands across 4 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, 20 β-strands

Element	Residues	Length	Sheet
β-strand	8-11	4	1
β-strand	16-21	6	1
β-strand	24	1	2
β-strand	29-32	4	1
β-strand	35-38	4	3
α-helix	41-43	3
α-helix	45-47	3
β-strand	53-54	2	3
α-helix	56-59	4
β-strand	65-68	4	3
β-strand	71-72	2	4
β-strand	75-76	2	4
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	1
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	1
α-helix	137-143	7
β-strand	150-155	6	5
β-strand	160-166	7	5
β-strand	169-170	2	5
β-strand	176-178	3	5
α-helix	182-196	15
α-helix	203-216	14
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	259-262	4
α-helix	272-273	2
α-helix	274-283	10
α-helix	290-295	6
β-strand	297-300	4	5
α-helix	302-304	3
α-helix	310-320	11
β-strand	329-330	2	5
α-helix	338-347	10
α-helix	350-353	4
β-strand	357-358	2	1
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain B: 26 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	8-12	5	7
β-strand	16-21	6	7
β-strand	24	1	8
β-strand	29-32	4	7
β-strand	35-38	4	9
α-helix	41-43	3
α-helix	45-47	3
β-strand	53-54	2	9
α-helix	56-59	4
β-strand	65-68	4	9
β-strand	71-72	2	10
β-strand	75-76	2	10
α-helix	79-88	10
α-helix	89-93	5
α-helix	98-100	3
β-strand	103-107	5	7
α-helix	113-121	9
α-helix	122-126	5
β-strand	131-136	6	7
α-helix	137-144	8
β-strand	150-155	6	11
β-strand	160-166	7	11
β-strand	169-170	2	11
β-strand	176-177	2	11
α-helix	182-196	15
α-helix	203-216	14
α-helix	223-232	10
α-helix	234-236	3
β-strand	238-241	4	12
β-strand	247-250	4	12
α-helix	253-256	4
α-helix	259-262	4
α-helix	264-266	3
α-helix	272-273	2
α-helix	274-283	10
α-helix	287-295	9
β-strand	297-298	2	13
β-strand	299-300	2	11
α-helix	302-305	4
α-helix	310-320	11
β-strand	329-330	2	13
α-helix	338-347	10
α-helix	350-353	4
β-strand	357-358	2	7
α-helix	359-365	7
α-helix	367-369	3
α-helix	370-373	4

Chain D: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	435-443	9
β-strand	448	1	2

Chain E: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	436-443	8
α-helix	447	1
β-strand	448	1	8
α-helix	449	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Actin, alpha skeletal muscle	A, B	protein	375	ORYCTOLAGUS CUNICULUS	P68135 (AlphaFold model)
Neural wiskott-aldrich syndrome protein	D, E	protein	93	HOMO SAPIENS	O00401 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2VCP_1 ACTIN, ALPHA SKELETAL MUSCLE (chains A, B)
DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT
QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL
AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ
EYDEAGPSIVHRKCF

Sequence of entity 2 (D, E), FASTA

>2VCP_2 NEURAL WISKOTT-ALDRICH SYNDROME PROTEIN (chains D, E)
PSDGDHQVPTTAGNKAALLDQIREGAQLKKVEQNSRPVSCSGRDALLDQIRQGIQLKSVA
DGQESTPPTPAPTSGIVGALMEVMQKRSKAIHS

Ligands and cofactors

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

Primary citation

Interactions of isolated C-terminal fragments of neural Wiskott-Aldrich syndrome protein (N-WASP) with actin and Arp2/3 complex. Gaucher, J.F., Mauge, C., Didry, D. et al. J Biol Chem (2012) 287:34646-34659. DOI 10.1074/jbc.M112.394361 · 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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