1RKC: Human vinculin head

Human vinculin head (1-258) in complex with talin's vinculin binding site 3 (residues 1944-1969). Determined by X-ray diffraction at 2.7 Å resolution. Released 13 Jan 2004.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Homo sapiens, Gallus gallus
Chains: 2
Atoms: 2,223
Mol. weight: 32.4 kDa
Released: 13 Jan 2004

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

Secondary structure: helices and β-sheets

1RKC contains 16 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: 14 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	6	1	1
α-helix	7-13	7
α-helix	15-25	11
α-helix	38-40	3
α-helix	53-63	11
α-helix	68-71	4
α-helix	74-82	9
α-helix	84-87	4
α-helix	91-93	3
α-helix	104-106	3
α-helix	108-147	40
α-helix	148-150	3
α-helix	154-179	26
β-strand	182	1	1
α-helix	185-215	31
α-helix	224-251	28

Chain B: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1948-1963	16
α-helix	1965-1967	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Vinculin	A	protein	262	Homo sapiens	P18206 (AlphaFold model)
Talin	B	protein	26	Gallus gallus	P54939 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1RKC_1 Vinculin (chains A)
HHHHMPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVR
VGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGIL
SGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMID
ERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEK
MSAEINEIIRVLQLTSWDEDAW

Sequence of entity 2 (B), FASTA

>1RKC_2 Talin (chains B)
YTKKELIESARKVSEKVSHVLAALQA

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…
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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