Crystal structure of Ang1-A451D receptor binding domain. Determined by X-ray diffraction at 2.28 Å resolution. Released 2 Jul 2025.
Explore 9IVU in 3D Show helices and sheets RCSB PDB PDBe
9IVU contains 9 α-helices and 21 β-strands across 1 chain. 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 | 286-291 | 6 | |
| β-strand | 298-302 | 5 | 1 |
| β-strand | 311-316 | 6 | 1 |
| α-helix | 319-321 | 3 | |
| β-strand | 324-330 | 7 | 1 |
| α-helix | 341-346 | 6 | |
| β-strand | 348-349 | 2 | 1 |
| β-strand | 355-356 | 2 | 1 |
| α-helix | 359-367 | 9 | |
| β-strand | 371-378 | 8 | 1 |
| β-strand | 384-394 | 11 | 1 |
| α-helix | 397-399 | 3 | |
| β-strand | 403-410 | 8 | 1 |
| β-strand | 423 | 1 | 1 |
| β-strand | 426 | 1 | 2 |
| β-strand | 427 | 1 | 3 |
| β-strand | 430 | 1 | 3 |
| α-helix | 439-443 | 5 | |
| β-strand | 447 | 1 | 2 |
| β-strand | 450 | 1 | 4 |
| β-strand | 452 | 1 | 4 |
| β-strand | 455-456 | 2 | 5 |
| α-helix | 464-467 | 4 | |
| β-strand | 468 | 1 | 6 |
| β-strand | 475-476 | 2 | 5 |
| α-helix | 477-480 | 4 | |
| β-strand | 481 | 1 | 5 |
| β-strand | 484 | 1 | 6 |
| α-helix | 485-486 | 2 | |
| β-strand | 488-495 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Angiopoietin-1 | A | protein | 229 | Homo sapiens | Q15389 (AlphaFold model) |
>9IVU_1 Angiopoietin-1 (chains A) DYKDDDDKGGGGSFRDCADVYQAGFNKSGIYTIYINNMPEPKKVFCNMDVNGGGWTVIQH REDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQY DRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWF DDCGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
Development of a recombinant Ang1 variant with enhanced Tie2 binding and its application to attenuate sepsis in mice. Wang, R., Li, H., Xie, Z. et al. Sci Adv (2025) 11:eads1796-eads1796. DOI 10.1126/sciadv.ads1796 · PubMed
Other PDB entries of the same protein (UniProt Q15389 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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