Crystal structure of the vinculin tail and a pathway for activation. Determined by X-ray diffraction at 1.8 Å resolution. Released 4 Aug 2000.
Explore 1QKR in 3D Show helices and sheets RCSB PDB PDBe
1QKR contains 18 α-helices and 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 882-889 | 8 | |
| α-helix | 892-895 | 4 | |
| α-helix | 897-909 | 13 | |
| β-strand | 912 | 1 | 1 |
| α-helix | 918-936 | 19 | |
| α-helix | 941-943 | 3 | |
| α-helix | 944-971 | 28 | |
| α-helix | 975-985 | 11 | |
| α-helix | 988-1005 | 18 | |
| α-helix | 1013-1044 | 32 | |
| α-helix | 1052-1054 | 3 | |
| β-strand | 1060 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 886-889 | 4 | |
| α-helix | 892-895 | 4 | |
| α-helix | 897-909 | 13 | |
| β-strand | 912 | 1 | 2 |
| α-helix | 918-938 | 21 | |
| α-helix | 944-971 | 28 | |
| α-helix | 975-986 | 12 | |
| α-helix | 988-1005 | 18 | |
| α-helix | 1013-1044 | 32 | |
| β-strand | 1060 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vinculin | A, B | protein | 188 | GALLUS GALLUS | P12003 (AlphaFold model) |
>1QKR_1 VINCULIN (chains A, B) EEKDEEFPEQKAGEAINQPMMMAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVR GGSGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKIL STVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRW VRKTPWYQ
Crystal Structure of the Vinculin Tail and a Pathway for Activation. Bakolitsa, C., De Pereda, J.M., Bagshaw, C.R. et al. Cell (1999) 99:603. DOI 10.1016/S0092-8674(00)81549-4 · PubMed
Other PDB entries of the same protein (UniProt P12003 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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