Solution NMR structure of V-1 bound to capping protein (CP). Determined by solution NMR. Released 9 Jun 2010.
Explore 2KXP in 3D Show helices and sheets RCSB PDB PDBe
2KXP contains 32 α-helices and 27 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 |
|---|---|---|---|
| α-helix | 10-21 | 12 | |
| α-helix | 24-25 | 2 | |
| α-helix | 29-40 | 12 | |
| α-helix | 43-48 | 6 | |
| α-helix | 51-60 | 10 | |
| β-strand | 63-64 | 2 | 1 |
| β-strand | 75-76 | 2 | 1 |
| β-strand | 81 | 1 | 2 |
| β-strand | 86-87 | 2 | 2 |
| β-strand | 94-95 | 2 | 3 |
| β-strand | 96-97 | 2 | 2 |
| β-strand | 109-110 | 2 | 3 |
| α-helix | 118-132 | 15 | |
| β-strand | 139-148 | 10 | 4 |
| β-strand | 151-161 | 11 | 4 |
| α-helix | 165-167 | 3 | |
| β-strand | 170-179 | 10 | 4 |
| β-strand | 190-198 | 9 | 4 |
| β-strand | 202 | 1 | 5 |
| β-strand | 204-212 | 9 | 4 |
| α-helix | 216-218 | 3 | |
| α-helix | 221-249 | 29 | |
| α-helix | 250-254 | 5 | |
| α-helix | 255-258 | 4 | |
| α-helix | 271-274 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 303-313 | 11 | |
| α-helix | 318-320 | 3 | |
| α-helix | 321-331 | 11 | |
| α-helix | 333-335 | 3 | |
| α-helix | 336-339 | 4 | |
| α-helix | 347-348 | 2 | |
| β-strand | 349-352 | 4 | 6 |
| β-strand | 357-360 | 4 | 6 |
| β-strand | 366-367 | 2 | 7 |
| β-strand | 370-371 | 2 | 7 |
| β-strand | 372 | 1 | 8 |
| β-strand | 379 | 1 | 8 |
| α-helix | 391-411 | 21 | |
| β-strand | 416-423 | 8 | 4 |
| β-strand | 428-437 | 10 | 4 |
| β-strand | 444-456 | 13 | 4 |
| β-strand | 457 | 1 | 5 |
| β-strand | 465-473 | 9 | 5 |
| β-strand | 474-479 | 6 | 4 |
| β-strand | 486-490 | 5 | 4 |
| β-strand | 493-501 | 9 | 5 |
| α-helix | 509-530 | 22 | |
| α-helix | 531-536 | 6 | |
| α-helix | 537-543 | 7 | |
| α-helix | 553-567 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 603-607 | 5 | |
| α-helix | 609-612 | 4 | |
| α-helix | 615-622 | 8 | |
| α-helix | 640-645 | 6 | |
| α-helix | 653-656 | 4 | |
| α-helix | 671-676 | 6 | |
| α-helix | 682-688 | 7 | |
| α-helix | 702-706 | 5 | |
| α-helix | 711-714 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| F-actin-capping protein subunit alpha-1 | A | protein | 275 | Gallus gallus | P13127 (AlphaFold model) |
| F-actin-capping protein subunit beta isoforms 1 and 2 | B | protein | 270 | Gallus gallus | P14315 (AlphaFold model) |
| Myotrophin | C | protein | 118 | Mus musculus | P62774 (AlphaFold model) |
>2KXP_1 F-actin-capping protein subunit alpha-1 (chains A) RVSDEEKVRIAAKFITHAPPGEFNEVFNDVRLLLNNDNLLREGAAHAFAQYNMDQFTPVK IEGYDDQVLITEHGDLGNGRFLDPRNKISFKFDHLRKEASDPQPEDTESALKQWRDACDS ALRAYVKDHYPNGFCTVYGKSIDGQQTIIACIESHQFQPKNFWNGRWRSEWKFTITPPTA QVAAVLKIQVHYYEDGNVQLVSHKDIQDSVQVSSDVQTAKEFIKIIENAENEYQTAISEN YQTMSDTTFKALRRQLPVTRTKIDWNKILSYKIGK
>2KXP_2 F-actin-capping protein subunit beta isoforms 1 and 2 (chains B) SDQQLDCALDLMRRLPPQQIEKNLSDLIDLVPSLCEDLLSSVDQPLKIARDKVVGKDYLL CDYNRDGDSYRSPWSNKYDPPLEDGAMPSARLRKLEVEANNAFDQYRDLYFEGGVSSVYL WDLDHGFAGVILIKKAGDGSKKIKGCWDSIHVVEVQEKSSGRTAHYKLTSTVMLWLQTNK TGSGTMNLGGSLTRQMEKDETVSDSSPHIANIGRLVEDMENKIRSTLNEIYFGKTKDIVN GLRSIDAIPDNQKYKQLQRELSQVLTQRQI
>2KXP_3 Myotrophin (chains C) MCDKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGAD INAPDKHHITPLLSAVYEGHVSCVKLLLSKGADKTVKGPDGLTALEATDNQAIKALLQ
Solution NMR structure of V-1 bound to capping protein (CP). Zwolak, A., Fujiwara, I., Hammer III, J.A. et al. To be published.
Other PDB entries of the same protein (UniProt P13127 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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