Crystal structure of Snx9PX-BAR (230-595), H32. Determined by X-ray diffraction at 4.1 Å resolution. Released 16 Sept 2008.
Explore 3DYU in 3D Show helices and sheets RCSB PDB PDBe
3DYU contains 42 α-helices and 22 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 | 232-235 | 4 | 1 |
| β-strand | 242-243 | 2 | 1 |
| β-strand | 252-259 | 8 | 2 |
| β-strand | 270-276 | 7 | 2 |
| β-strand | 283-286 | 4 | 2 |
| α-helix | 287-301 | 15 | |
| α-helix | 309-312 | 4 | |
| α-helix | 321-339 | 19 | |
| α-helix | 348-354 | 7 | |
| α-helix | 361-370 | 10 | |
| α-helix | 376-382 | 7 | |
| β-strand | 383-385 | 3 | 1 |
| α-helix | 392-427 | 36 | |
| α-helix | 430-449 | 20 | |
| α-helix | 459-479 | 21 | |
| α-helix | 482-484 | 3 | |
| α-helix | 486-501 | 16 | |
| α-helix | 505-507 | 3 | |
| α-helix | 510-516 | 7 | |
| α-helix | 519-525 | 7 | |
| α-helix | 531-589 | 59 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 232-235 | 4 | 3 |
| β-strand | 242-243 | 2 | 3 |
| β-strand | 252-259 | 8 | 4 |
| β-strand | 270-276 | 7 | 4 |
| β-strand | 283-286 | 4 | 4 |
| α-helix | 287-301 | 15 | |
| α-helix | 309-312 | 4 | |
| α-helix | 321-339 | 19 | |
| α-helix | 348-354 | 7 | |
| α-helix | 361-370 | 10 | |
| α-helix | 376-382 | 7 | |
| β-strand | 383-385 | 3 | 3 |
| α-helix | 392-427 | 36 | |
| α-helix | 430-449 | 20 | |
| α-helix | 459-479 | 21 | |
| α-helix | 482-484 | 3 | |
| α-helix | 486-501 | 16 | |
| α-helix | 503-516 | 14 | |
| α-helix | 519-525 | 7 | |
| α-helix | 531-589 | 59 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 232-235 | 4 | 5 |
| β-strand | 242-243 | 2 | 5 |
| β-strand | 252-254 | 3 | 6 |
| β-strand | 259 | 1 | 7 |
| β-strand | 270 | 1 | 7 |
| β-strand | 271 | 1 | 8 |
| β-strand | 274-276 | 3 | 6 |
| β-strand | 283 | 1 | 6 |
| β-strand | 286 | 1 | 8 |
| α-helix | 287-301 | 15 | |
| α-helix | 321-339 | 19 | |
| α-helix | 348-354 | 7 | |
| α-helix | 361-370 | 10 | |
| α-helix | 376-382 | 7 | |
| β-strand | 383-385 | 3 | 5 |
| α-helix | 392-427 | 36 | |
| α-helix | 430-449 | 20 | |
| α-helix | 459-479 | 21 | |
| α-helix | 482-484 | 3 | |
| α-helix | 486-501 | 16 | |
| α-helix | 503-516 | 14 | |
| α-helix | 519-525 | 7 | |
| α-helix | 531-589 | 59 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sorting nexin-9 | A, B, C | protein | 366 | Homo sapiens | Q9Y5X1 (AlphaFold model) |
>3DYU_1 Sorting nexin-9 (chains A, B, C) EKIPIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKH FDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVISESEV FQQFLNFRDEKEWKTGKRKAERDELAGVMIFSTMEPEAPDLDLVEIEQKCEAVGKFTKAM DDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLATVFSSSGYQGETDLNDAITEAGK TYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGTHKGAIEKVKESDKLVATSKI TLQDKQNMVKRVSIMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQAL SRFPVM
Structure and plasticity of endophilin and sorting nexin 9. Wang, Q., Kaan, H.Y., Hooda, R.N. et al. Structure (2008) 16:1574-1587. DOI 10.1016/j.str.2008.07.016 · PubMed
Other PDB entries of the same protein (UniProt Q9Y5X1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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