MDFF model of the vinculin tail domain bound to F-actin. Determined by electron microscopy at 8.5 Å resolution. Released 4 Nov 2015.
Explore 3JBI in 3D Show helices and sheets RCSB PDB PDBe
3JBI contains 47 α-helices and 39 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 8-11 | 4 | 1 |
| β-strand | 17-21 | 5 | 1 |
| β-strand | 29-31 | 3 | 1 |
| β-strand | 35-37 | 3 | 2 |
| α-helix | 41 | 1 | |
| β-strand | 42 | 1 | 3 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 57-60 | 4 | |
| β-strand | 66-68 | 3 | 2 |
| β-strand | 71-72 | 2 | 4 |
| β-strand | 75-76 | 2 | 4 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 115-127 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-156 | 7 | 5 |
| β-strand | 159-166 | 8 | 5 |
| β-strand | 169-170 | 2 | 5 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 5 |
| α-helix | 183-194 | 12 | |
| α-helix | 203-215 | 13 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 6 |
| β-strand | 247-250 | 4 | 6 |
| α-helix | 252-259 | 8 | |
| α-helix | 264-266 | 3 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-293 | 7 | |
| β-strand | 297-300 | 4 | 5 |
| α-helix | 302-304 | 3 | |
| α-helix | 311-320 | 10 | |
| α-helix | 322 | 1 | |
| β-strand | 329-330 | 2 | 5 |
| α-helix | 335-337 | 3 | |
| α-helix | 338-348 | 11 | |
| α-helix | 352-355 | 4 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-365 | 7 | |
| α-helix | 366-370 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-11 | 4 | 7 |
| β-strand | 17-21 | 5 | 7 |
| β-strand | 29-31 | 3 | 7 |
| β-strand | 35-38 | 4 | 8 |
| β-strand | 53-54 | 2 | 8 |
| α-helix | 57-60 | 4 | |
| β-strand | 65-68 | 4 | 8 |
| β-strand | 71-72 | 2 | 9 |
| β-strand | 75-76 | 2 | 9 |
| α-helix | 79-87 | 9 | |
| α-helix | 88-94 | 7 | |
| β-strand | 103-107 | 5 | 7 |
| α-helix | 115-127 | 13 | |
| β-strand | 131-132 | 2 | 10 |
| β-strand | 134-136 | 3 | 7 |
| α-helix | 137-143 | 7 | |
| β-strand | 149-156 | 8 | 3 |
| β-strand | 159-166 | 8 | 3 |
| β-strand | 169-170 | 2 | 3 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 3 |
| α-helix | 183-193 | 11 | |
| α-helix | 194-196 | 3 | |
| α-helix | 203-215 | 13 | |
| α-helix | 223-231 | 9 | |
| β-strand | 238-241 | 4 | 11 |
| β-strand | 247-250 | 4 | 11 |
| α-helix | 252-259 | 8 | |
| α-helix | 274-282 | 9 | |
| α-helix | 287-293 | 7 | |
| β-strand | 297-300 | 4 | 3 |
| α-helix | 302-304 | 3 | |
| α-helix | 311-320 | 10 | |
| α-helix | 322 | 1 | |
| α-helix | 335-348 | 14 | |
| α-helix | 352-355 | 4 | |
| β-strand | 357-358 | 2 | 10 |
| α-helix | 359-365 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 918-938 | 21 | |
| α-helix | 941-943 | 3 | |
| α-helix | 944-971 | 28 | |
| α-helix | 975-985 | 11 | |
| α-helix | 987-1005 | 19 | |
| α-helix | 1013-1044 | 32 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin, alpha skeletal muscle | A, B | protein | 375 | Oryctolagus cuniculus | P68135 (AlphaFold model) |
| Vinculin | V | protein | 254 | Gallus gallus | P12003 (AlphaFold model) |
>3JBI_1 Actin, alpha skeletal muscle (chains A, B) DEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS KRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMT QIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDL AGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSY ELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMS GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQ EYDEAGPSIVHRKCF
>3JBI_2 Vinculin (chains V) GSEEKDEEFPEQKAGEAINQPMMMAARQLHDEARKWSSKPVTVINEAAEAGVDIDEEDDA DVEFSLPSDIEDDYEPELLLMPTNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMA LLMAEMSRLVRGGSGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCER IPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIK IRTDAGFTLRWVRK
The Structural Basis of Actin Organization by Vinculin and Metavinculin. Kim, L.Y., Thompson, P.M., Lee, H.T. et al. J Mol Biol (2016) 428:10-25. DOI 10.1016/j.jmb.2015.09.031 · PubMed
Other PDB entries of the same protein (UniProt P68135 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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