Crystal structure of talin autoinhibition complex. Determined by X-ray diffraction at 2.05 Å resolution. Released 4 Jul 2012.
Explore 4F7G in 3D Show helices and sheets RCSB PDB PDBe
4F7G contains 16 α-helices and 9 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 | 211-224 | 14 | |
| α-helix | 232-247 | 16 | |
| α-helix | 262-264 | 3 | |
| α-helix | 268-273 | 6 | |
| α-helix | 276-284 | 9 | |
| α-helix | 291-303 | 13 | |
| β-strand | 311-318 | 8 | 1 |
| α-helix | 319 | 1 | |
| β-strand | 325-332 | 8 | 1 |
| β-strand | 336-340 | 5 | 1 |
| β-strand | 347-352 | 6 | 1 |
| α-helix | 353-355 | 3 | |
| β-strand | 358-361 | 4 | 1 |
| β-strand | 365-369 | 5 | 1 |
| β-strand | 372 | 1 | 2 |
| β-strand | 374 | 1 | 2 |
| β-strand | 378-381 | 4 | 1 |
| α-helix | 385-398 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1658-1683 | 26 | |
| α-helix | 1688-1691 | 4 | |
| α-helix | 1695-1722 | 28 | |
| α-helix | 1724-1736 | 13 | |
| α-helix | 1738-1751 | 14 | |
| α-helix | 1755-1782 | 28 | |
| α-helix | 1790-1820 | 31 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Talin-1 | A | protein | 222 | Mus musculus | P26039 (AlphaFold model) |
| Talin-1 | B | protein | 216 | Mus musculus | P26039 (AlphaFold model) |
>4F7G_1 Talin-1 (chains A) MHHHHHHSSGVDLGTENLYFQSSRDPVQLNLLYVQARDDILNGSHPVSFDKACEFAGFQC QIQFGPHNEQKHKAGFLDLKDFLPKEYVKQKGERKIFQAHKNCGQMSEIEAKVRYVKLAR SLKTYGVSFFLVKEKMKGKNKLVPRLLGITKECVMRVDEKTKEVIQEWSLTNIKRWAASP KSFTLDFGDYQDGYYSVQTTEGEQIAQLIAGYIDIILKKKKS
>4F7G_2 Talin-1 (chains B) MHHHHHHSSGVDLGTENLYFQSKAPGQLECETAIAALNSCLRDLDQASLAAVSQQLAPRE GISQEALHTQMLTAVQEISHLIEPLASAARAEASQLGHKVSQMAQYFEPLTLAAVGAASK TLSHPQQMALLDQTKTLAESALQLLYTAKEAGGNPKQAAHTQEALEEAVQMMTEAVEDLT TTLNEAASAAGVVGGMVDSITQAINQLDEGPMGDPE
A novel membrane-dependent on/off switch mechanism of talin FERM domain at sites of cell adhesion. Song, X., Yang, J., Hirbawi, J. et al. Cell Res (2012) 22:1533-1545. DOI 10.1038/cr.2012.97 · PubMed
Other PDB entries of the same protein (UniProt P26039 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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