The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Thr-Val linker variant, at 1.2 Angstrom resolution. Determined by X-ray diffraction at 1.19 Å resolution. Released 6 Nov 2024.
Explore 9DOC in 3D Show helices and sheets RCSB PDB PDBe
9DOC contains 17 α-helices and 6 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 | 18-20 | 3 | |
| α-helix | 24-26 | 3 | |
| α-helix | 29-43 | 15 | |
| α-helix | 45-49 | 5 | |
| α-helix | 57-60 | 4 | |
| α-helix | 65-71 | 7 | |
| α-helix | 76-88 | 13 | |
| β-strand | 94-101 | 8 | 1 |
| α-helix | 104-109 | 6 | |
| α-helix | 110-123 | 14 | |
| β-strand | 129-136 | 8 | 1 |
| β-strand | 140-147 | 8 | 1 |
| α-helix | 150-161 | 12 | |
| α-helix | 171-185 | 15 | |
| α-helix | 187-189 | 3 | |
| β-strand | 192-198 | 7 | 1 |
| α-helix | 206-219 | 14 | |
| β-strand | 223-228 | 6 | 1 |
| α-helix | 234-240 | 7 | |
| α-helix | 244-246 | 3 | |
| β-strand | 247-249 | 3 | 1 |
| α-helix | 250-252 | 3 | |
| α-helix | 253-265 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription factor ETV6,Capillary morphogenesis gene 2 protein | A | protein | 268 | Homo sapiens | P41212 (AlphaFold model), P58335 (AlphaFold model) |
>9DOC_1 Transcription factor ETV6,Capillary morphogenesis gene 2 protein (chains A) MGHHHHHHHHHHSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLSPIDSNTFEMNGKAL LLLTKEDFRYRSPHSGDELYELLQHILAQARTVFDLYFVLDKSGSVANNWIEIYNFVQQL AERFVSPEMRLSFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGETYIHEGLKLANE QIQKAGGLKTSSIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYAVGVLDFEQAQLERI ADSKEQVFPVKGGFQALKGIINSILAQS
Water and common crystallization additives (NA, GOL) are not listed.
1TEL Fusions Outperform 2TEL and 3TEL Fusions in Controlled Comparisons. Samarawickrama, P., Ludlow, K., Probst, R. et al. To be published.
Other PDB entries of the same protein (UniProt P41212 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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