Crystal structure of DhhN bound to BOCFn3. Determined by X-ray diffraction at 1.9 Å resolution. Released 2 Jun 2010.
Explore 3N1G in 3D Show helices and sheets RCSB PDB PDBe
3N1G contains 24 α-helices and 32 β-strands across 4 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 | 41-44 | 4 | |
| β-strand | 48-49 | 2 | 5 |
| α-helix | 66-68 | 3 | |
| α-helix | 72-75 | 4 | |
| β-strand | 78-79 | 2 | 6 |
| β-strand | 85-87 | 3 | 5 |
| α-helix | 95-97 | 3 | |
| β-strand | 98-99 | 2 | 6 |
| α-helix | 101-117 | 17 | |
| β-strand | 123-127 | 5 | 5 |
| α-helix | 136 | 1 | |
| α-helix | 140-143 | 4 | |
| β-strand | 146-151 | 6 | 5 |
| α-helix | 156-158 | 3 | |
| α-helix | 159-168 | 10 | |
| β-strand | 173-175 | 3 | 5 |
| β-strand | 182-185 | 4 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42-44 | 3 | |
| β-strand | 48-49 | 2 | 1 |
| α-helix | 66-68 | 3 | |
| α-helix | 72-75 | 4 | |
| β-strand | 78-79 | 2 | 2 |
| β-strand | 85-87 | 3 | 1 |
| α-helix | 95-97 | 3 | |
| β-strand | 98-99 | 2 | 2 |
| α-helix | 101-117 | 17 | |
| β-strand | 123-127 | 5 | 1 |
| α-helix | 136 | 1 | |
| α-helix | 140-143 | 4 | |
| β-strand | 146-151 | 6 | 1 |
| α-helix | 156-158 | 3 | |
| α-helix | 159-168 | 10 | |
| β-strand | 173-175 | 3 | 1 |
| β-strand | 182-185 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 717-725 | 9 | 3 |
| β-strand | 728-734 | 7 | 3 |
| α-helix | 737-740 | 4 | |
| β-strand | 747-754 | 8 | 4 |
| α-helix | 760-762 | 3 | |
| β-strand | 764-769 | 6 | 4 |
| β-strand | 774-777 | 4 | 3 |
| β-strand | 785-793 | 9 | 4 |
| β-strand | 798 | 1 | 4 |
| α-helix | 799-801 | 3 | |
| β-strand | 805-808 | 4 | 4 |
| α-helix | 809-811 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 717-723 | 7 | 7 |
| β-strand | 729-734 | 6 | 7 |
| β-strand | 747-754 | 8 | 8 |
| α-helix | 760-762 | 3 | |
| β-strand | 764-769 | 6 | 8 |
| β-strand | 774-777 | 4 | 7 |
| β-strand | 785-793 | 9 | 8 |
| β-strand | 798 | 1 | 8 |
| β-strand | 805-808 | 4 | 8 |
| α-helix | 809-812 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Desert hedgehog protein | A, B | protein | 170 | Homo sapiens | O43323 (AlphaFold model) |
| Brother of CDO | C, D | protein | 111 | Homo sapiens | Q9BWV1 (AlphaFold model) |
>3N1G_1 Desert hedgehog protein (chains A, B) GSGPGPGRGPVGRRRYARKQLVPLLYKQFVPGVPERTLGASGPAEGRVARGSERFRDLVP NYNPDIIFKDEENSGADRLMTERCKERVNALAIAVMNMWPGVRLRVTEGWDEDGHHAQDS LHYEGRALDITTSDRDRNKYGLLARLAVEAGFDWVYYESRNHVHVSVKAD
>3N1G_2 Brother of CDO (chains C, D) GSTERPVAGPYITFTDAVNETTIMLKWMYIPASNNNTPIHGFYIYYRPTDSDNDSDYKKD MVEGDKYWHSISHLQPETSYDIKMQCFNEGGESEFSNVMICETKARKSSGQ
All mammalian Hedgehog proteins interact with cell adhesion molecule, down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a conserved manner. Kavran, J.M., Ward, M.D., Oladosu, O.O. et al. J Biol Chem (2010) 285:24584-24590. DOI 10.1074/jbc.M110.131680 · PubMed
Other PDB entries of the same protein (UniProt O43323 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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