The Calcium-Activated C-terminal half of gelsolin. Determined by X-ray diffraction at 2.0 Å resolution. Released 14 Oct 2003.
Explore 1P8X in 3D Show helices and sheets RCSB PDB PDBe
1P8X contains 41 α-helices and 56 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 | 420-426 | 7 | 1 |
| β-strand | 429-432 | 4 | 1 |
| α-helix | 433-434 | 2 | |
| α-helix | 435-437 | 3 | |
| β-strand | 440-442 | 3 | 2 |
| β-strand | 446-455 | 10 | 1 |
| β-strand | 458-467 | 10 | 1 |
| α-helix | 473-489 | 17 | |
| β-strand | 495-500 | 6 | 1 |
| α-helix | 506-510 | 5 | |
| α-helix | 515-516 | 2 | |
| β-strand | 517-520 | 4 | 2 |
| α-helix | 530-534 | 5 | |
| β-strand | 537-543 | 7 | 2 |
| β-strand | 549-554 | 6 | 2 |
| α-helix | 558-560 | 3 | |
| β-strand | 562 | 1 | 3 |
| β-strand | 566-570 | 5 | 2 |
| β-strand | 575-579 | 5 | 2 |
| α-helix | 585-597 | 13 | |
| α-helix | 601-602 | 2 | |
| β-strand | 603-606 | 4 | 2 |
| α-helix | 612-617 | 6 | |
| β-strand | 625 | 1 | 3 |
| α-helix | 628-631 | 4 | |
| β-strand | 641-644 | 4 | 4 |
| α-helix | 663-665 | 3 | |
| β-strand | 671-675 | 5 | 4 |
| β-strand | 680-684 | 5 | 4 |
| α-helix | 690-706 | 17 | |
| β-strand | 717-721 | 5 | 4 |
| α-helix | 727-730 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 420-426 | 7 | 5 |
| β-strand | 429-432 | 4 | 5 |
| α-helix | 435-437 | 3 | |
| β-strand | 440-442 | 3 | 6 |
| β-strand | 446-452 | 7 | 5 |
| β-strand | 461-467 | 7 | 5 |
| α-helix | 473-489 | 17 | |
| β-strand | 495-500 | 6 | 5 |
| α-helix | 506-510 | 5 | |
| α-helix | 515-516 | 2 | |
| β-strand | 517-520 | 4 | 6 |
| α-helix | 530-534 | 5 | |
| β-strand | 537-543 | 7 | 6 |
| β-strand | 549-554 | 6 | 6 |
| α-helix | 558-560 | 3 | |
| β-strand | 562 | 1 | 7 |
| β-strand | 566-570 | 5 | 6 |
| β-strand | 575-579 | 5 | 6 |
| α-helix | 585-597 | 13 | |
| α-helix | 601-602 | 2 | |
| β-strand | 603-606 | 4 | 6 |
| α-helix | 612-617 | 6 | |
| β-strand | 625 | 1 | 7 |
| α-helix | 628-631 | 4 | |
| β-strand | 641-646 | 6 | 8 |
| β-strand | 653-656 | 4 | 8 |
| α-helix | 663-665 | 3 | |
| β-strand | 671-675 | 5 | 8 |
| β-strand | 680-684 | 5 | 8 |
| α-helix | 690-705 | 16 | |
| α-helix | 708-710 | 3 | |
| β-strand | 717-721 | 5 | 8 |
| α-helix | 727-730 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 420-426 | 7 | 9 |
| β-strand | 429-432 | 4 | 9 |
| α-helix | 435-437 | 3 | |
| β-strand | 440-442 | 3 | 10 |
| β-strand | 446-452 | 7 | 9 |
| β-strand | 461-467 | 7 | 9 |
| α-helix | 473-489 | 17 | |
| β-strand | 495-500 | 6 | 9 |
| α-helix | 506-510 | 5 | |
| α-helix | 515-516 | 2 | |
| β-strand | 517-520 | 4 | 10 |
| α-helix | 531-534 | 4 | |
| β-strand | 537-543 | 7 | 10 |
| β-strand | 549-554 | 6 | 10 |
| α-helix | 558-560 | 3 | |
| β-strand | 562 | 1 | 11 |
| β-strand | 566-570 | 5 | 10 |
| β-strand | 575-579 | 5 | 10 |
| α-helix | 585-597 | 13 | |
| β-strand | 603-606 | 4 | 10 |
| α-helix | 612-617 | 6 | |
| β-strand | 625 | 1 | 11 |
| α-helix | 628-631 | 4 | |
| β-strand | 641-646 | 6 | 12 |
| β-strand | 653-657 | 5 | 12 |
| α-helix | 663-665 | 3 | |
| β-strand | 671-675 | 5 | 12 |
| β-strand | 680-684 | 5 | 12 |
| α-helix | 690-705 | 16 | |
| α-helix | 708-710 | 3 | |
| β-strand | 717-721 | 5 | 12 |
| α-helix | 727-730 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gelsolin precursor, plasma | A, B, C | protein | 344 | Homo sapiens | P06396 (AlphaFold model) |
>1P8X_1 Gelsolin precursor, plasma (chains A, B, C) MDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQS TQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGGTSREGGQT APASTRLFQVRANSAGATRAVEVLPKAGALNSNDAFVLKTPSAAYLWVGTGASEAEKTGA QELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGR FVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEEEKTEALTSAKRYIETDPANR DRRTPITVVKQGFEPPSFVGWFLGWDDDYWSVDPLDRAMAELAA
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 9 |
Activation in isolation: Exposure of the actin-binding site in the C-terminal half of gelsolin does not require actin. Narayan, K., Chumnarnsilpa, S., Choe, H. et al. FEBS Lett (2003) 552:82-85. DOI 10.1016/S0014-5793(03)00933-5 · PubMed
Other PDB entries of the same protein (UniProt P06396 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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