1RKE: Human vinculin head

Human vinculin head (1-258) in complex with human vinculin tail (879-1066). Determined by X-ray diffraction at 2.35 Å resolution. Released 13 Jan 2004.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,660
Mol. weight: 50.33 kDa
Released: 13 Jan 2004

Explore 1RKE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1RKE contains 17 α-helices and 6 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: 12 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	-1-2	4
β-strand	6	1	1
α-helix	7-28	22
α-helix	29-33	5
α-helix	35-37	3
α-helix	41-59	19
α-helix	68-95	28
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	224-247	24
α-helix	253-255	3

Chain B: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	896-909	14
β-strand	912	1	2
α-helix	918-934	17
α-helix	944-970	27
β-strand	972	1	3
α-helix	975-1003	29
α-helix	1014-1043	30
β-strand	1048	1	3
β-strand	1060	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vinculin	A	protein	262	Homo sapiens	P18206 (AlphaFold model)
VCL protein	B	protein	185	Homo sapiens	P18206 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1RKE_1 Vinculin (chains A)
HHHHMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVR
VGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGIL
SGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMID
ERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEK
MSAEINEIIRVLQLTSWDEDAW

Sequence of entity 2 (B), FASTA

>1RKE_2 VCL protein (chains B)
DEEFPEQKAGEVINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRGGS
GTKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTV
KATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRK
TPWYQ

Primary citation

Vinculin activation by talin through helical bundle conversion. Izard, T., Evans, G., Borgon, R.A. et al. Nature (2004) 427:171-175. DOI 10.1038/nature02281 · 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…
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
9QWO 2.54 Å, Vinculin tail bound to paxillin LD2

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