The von Willebrand factor A domain of human capillary morphogenesis gene II, flexibly fused to the 1TEL crystallization chaperone, Thr-Val linker variant, Expressed with SUMO tag. Determined by X-ray diffraction at 1.9 Å resolution. Released 19 Jul 2023.
Explore 8FZU in 3D Show helices and sheets RCSB PDB PDBe
8FZU contains 47 α-helices and 18 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 | 8-10 | 3 | |
| α-helix | 13-15 | 3 | |
| α-helix | 18-31 | 14 | |
| α-helix | 34-36 | 3 | |
| α-helix | 46-51 | 6 | |
| α-helix | 54-60 | 7 | |
| α-helix | 65-77 | 13 | |
| β-strand | 83-90 | 8 | 1 |
| α-helix | 93-95 | 3 | |
| α-helix | 99-113 | 15 | |
| β-strand | 118-125 | 8 | 1 |
| β-strand | 129-136 | 8 | 1 |
| α-helix | 139-150 | 12 | |
| α-helix | 160-173 | 14 | |
| β-strand | 180-187 | 8 | 1 |
| α-helix | 195-208 | 14 | |
| β-strand | 212-217 | 6 | 1 |
| α-helix | 223-229 | 7 | |
| α-helix | 233-235 | 3 | |
| β-strand | 236-238 | 3 | 1 |
| α-helix | 242-253 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-10 | 4 | |
| α-helix | 13-15 | 3 | |
| α-helix | 18-32 | 15 | |
| α-helix | 34-36 | 3 | |
| α-helix | 46-51 | 6 | |
| α-helix | 54-60 | 7 | |
| α-helix | 65-78 | 14 | |
| β-strand | 83-90 | 8 | 2 |
| α-helix | 93-95 | 3 | |
| α-helix | 99-112 | 14 | |
| β-strand | 118-125 | 8 | 2 |
| β-strand | 129-136 | 8 | 2 |
| α-helix | 139-150 | 12 | |
| α-helix | 160-173 | 14 | |
| β-strand | 180-187 | 8 | 2 |
| α-helix | 195-208 | 14 | |
| β-strand | 212-217 | 6 | 2 |
| α-helix | 223-229 | 7 | |
| α-helix | 233-235 | 3 | |
| β-strand | 236-238 | 3 | 2 |
| α-helix | 239-254 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-6 | 4 | |
| α-helix | 8-10 | 3 | |
| α-helix | 13-15 | 3 | |
| α-helix | 18-32 | 15 | |
| α-helix | 34-38 | 5 | |
| α-helix | 46-51 | 6 | |
| α-helix | 54-60 | 7 | |
| α-helix | 65-78 | 14 | |
| β-strand | 83-90 | 8 | 3 |
| α-helix | 93-95 | 3 | |
| α-helix | 99-113 | 15 | |
| β-strand | 118-125 | 8 | 3 |
| β-strand | 129-136 | 8 | 3 |
| α-helix | 139-150 | 12 | |
| α-helix | 160-174 | 15 | |
| α-helix | 179 | 1 | |
| β-strand | 180-187 | 8 | 3 |
| α-helix | 195-208 | 14 | |
| β-strand | 212-217 | 6 | 3 |
| α-helix | 223-229 | 7 | |
| α-helix | 233-235 | 3 | |
| β-strand | 236-238 | 3 | 3 |
| α-helix | 242-254 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription factor ETV6,Anthrax toxin receptor 2 | A, B, C | protein | 257 | Homo sapiens | P41212 (AlphaFold model), P58335 (AlphaFold model) |
>8FZU_1 Transcription factor ETV6,Anthrax toxin receptor 2 (chains A, B, C) GSIALPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYR SPHSGDELYELLQHILAQARTVFDLYFVLDKSGSVANNWIEIYNFVQQLAERFVSPEMRL SFIVFSSQATIILPLTGDRGKISKGLEDLKRVSPVGETYIHEGLKLANEQIQKAGGLKTS SIIIALTDGKLDGLVPSYAEKEAKISRSLGASVYAVGVLDFEQAQLERIADSKEQVFPVK GGFQALKGIINSILAQS
Increasing the bulk of the 1TEL-target linker and retaining the 10×His tag in a 1TEL-CMG2-vWa construct improves crystal order and diffraction limits. Gajjar, P.L., Pedroza Romo, M.J., Litchfield, C.M. et al. Acta Crystallogr D Struct Biol (2023) 79:925-943. DOI 10.1107/S2059798323007246 · PubMed
Other PDB entries of the same protein (UniProt P41212 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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