2GWW: Human vinculin

Human vinculin (head domain, Vh1, residues 1-258) in complex with Shigella's IpaA vinculin binding site (residues 602-633). Determined by X-ray diffraction at 2.72 Å resolution. Released 14 Nov 2006.

Method: X-ray diffraction
Resolution: 2.72 Å
Organisms: Homo sapiens, Shigella flexneri
Chains: 2
Atoms: 2,282
Mol. weight: 33.34 kDa
Released: 14 Nov 2006

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

Secondary structure: helices and β-sheets

2GWW contains 11 α-helices and 2 β-strands across 2 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: 9 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	1
α-helix	7-28	22
α-helix	36-39	4
α-helix	43-64	22
α-helix	68-97	30
α-helix	102-147	46
α-helix	148-150	3
α-helix	154-179	26
β-strand	182	1	1
α-helix	185-216	32
α-helix	224-249	26

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	611-627	17
α-helix	628-630	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
vinculin	A	protein	266	Homo sapiens	P18206 (AlphaFold model)
IpaA	B	protein	30	Shigella flexneri	P18010 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2GWW_1 vinculin (chains A)
MEHHHHHHMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVS
NLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGS
RGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMA
KMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNF
TVEKMSAEINEIIRVLQLTSWDEDAW

Sequence of entity 2 (B), FASTA

>2GWW_2 IpaA (chains B)
NNDITAENNNIYKAAKDVTTSLSKVLKNIN

Primary citation

Shigella applies molecular mimicry to subvert vinculin and invade host cells. Izard, T., Tran Van Nhieu, G., Bois, P.R. J Cell Biol (2006) 175:465-475. DOI 10.1083/jcb.200605091 · PubMed

Other PDB entries of the same protein (UniProt P18206 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4LN2 1.0 Å, The second SH3 domain from CAP/Ponsin in complex with proline rich peptide from Vinculin
4LNP 1.41 Å, The first SH3 domain from CAP/Ponsin in complex with proline rich peptide from Vinculin
3RF3 1.61 Å, Shigella IpaA-VBS3 in complex with human vinculin
1YDI 1.8 Å, Human Vinculin Head Domain (VH1, 1-258) in Complex with Human Alpha-Actinin's…
3S90 1.97 Å, Human vinculin head domain Vh1 (residues 1-252) in complex with murine talin (VBS33;…
3TJ5 1.99 Å, human vinculin head domain (Vh1, residues 1-258) in complex with the vinculin binding…
3MYI 2.2 Å, Human metavinculin tail domain
4DJ9 2.25 Å, Human vinculin head domain Vh1 (residues 1-258) in complex with the talin vinculin…
1RKE 2.35 Å, Human vinculin head (1-258) in complex with human vinculin tail (879-1066)
1SYQ 2.42 Å, Human vinculin head domain VH1, residues 1-258, in complex with human talin's vinculin…
5L0I 2.45 Å, Human metavinculin MVt R975W cardiomyopathy-associated mutant (residues 959-1134)
3VF0 2.54 Å, Raver1 in complex with metavinculin L954 deletion mutant

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