Crystal Structure of IhhN bound to CDOFn3. Determined by X-ray diffraction at 1.6 Å resolution. Released 2 Jun 2010.
Explore 3N1F in 3D Show helices and sheets RCSB PDB PDBe
3N1F contains 22 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 | 46-48 | 3 | |
| β-strand | 52-53 | 2 | 1 |
| α-helix | 76-80 | 5 | |
| β-strand | 82-83 | 2 | 2 |
| β-strand | 89-91 | 3 | 1 |
| α-helix | 99-101 | 3 | |
| β-strand | 102-103 | 2 | 2 |
| α-helix | 105-121 | 17 | |
| β-strand | 127-131 | 5 | 1 |
| α-helix | 144-147 | 4 | |
| β-strand | 150-155 | 6 | 1 |
| α-helix | 160-162 | 3 | |
| α-helix | 163-172 | 10 | |
| β-strand | 177-182 | 6 | 1 |
| β-strand | 185-189 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 46-48 | 3 | |
| β-strand | 52-53 | 2 | 3 |
| α-helix | 77-80 | 4 | |
| β-strand | 82-83 | 2 | 4 |
| β-strand | 89-91 | 3 | 3 |
| α-helix | 99-101 | 3 | |
| β-strand | 102-103 | 2 | 4 |
| α-helix | 105-121 | 17 | |
| β-strand | 127-131 | 5 | 3 |
| α-helix | 144-147 | 4 | |
| β-strand | 150-155 | 6 | 3 |
| α-helix | 160-162 | 3 | |
| α-helix | 163-172 | 10 | |
| β-strand | 177-182 | 6 | 3 |
| β-strand | 185-189 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 829-830 | 2 | |
| β-strand | 831-837 | 7 | 5 |
| β-strand | 843-848 | 6 | 5 |
| β-strand | 861-868 | 8 | 6 |
| α-helix | 874-876 | 3 | |
| β-strand | 878-883 | 6 | 6 |
| β-strand | 888-891 | 4 | 5 |
| α-helix | 894-895 | 2 | |
| β-strand | 899-908 | 10 | 6 |
| β-strand | 911-912 | 2 | 6 |
| α-helix | 913-915 | 3 | |
| β-strand | 919-922 | 4 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 831-837 | 7 | 7 |
| β-strand | 843-848 | 6 | 7 |
| α-helix | 851-854 | 4 | |
| β-strand | 861-868 | 8 | 8 |
| α-helix | 874-876 | 3 | |
| β-strand | 878-883 | 6 | 8 |
| β-strand | 888-891 | 4 | 7 |
| α-helix | 894-895 | 2 | |
| β-strand | 899-908 | 10 | 8 |
| β-strand | 911-912 | 2 | 8 |
| α-helix | 913-915 | 3 | |
| β-strand | 919-922 | 4 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Indian hedgehog protein | A, B | protein | 169 | Homo sapiens | Q14623 (AlphaFold model) |
| Cell adhesion molecule-related/down-regulated by oncogenes | C, D | protein | 102 | Homo sapiens | Q4KMG0 (AlphaFold model) |
>3N1F_1 Indian hedgehog protein (chains A, B) GSGPGPGRVVGSRRRPPRKLVPLAYKQFSPNVPEKTLGASGRYEGKIARSSERFKELTPN YNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGVKLRVTEGWDEDGHHSEESL HYEGRAVDITTSDRDRNKYGLLARLAVEAGFDWVYYESKAHVHCSVKSE
>3N1F_2 Cell adhesion molecule-related/down-regulated by oncogenes (chains C, D) GSTPITGPHIAYTEAVSDTQIMLKWTYIPSSNNNTPIQGFYIYYRPTDSDNDSDYKRDVV EGSKQWHMIGHLQPETSYDIKMQCFNEGGESEFSNVMICETK
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 Q14623 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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