3N1Q: DhhN
Crystal Structure of DhhN bound to CDOFn3. Determined by X-ray diffraction at 2.89 Å resolution. Released 2 Jun 2010.
- Method
- X-ray diffraction
- Resolution
- 2.89 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 5,767
- Mol. weight
- 92.82 kDa
- Ligands
- ZN, CA
- Released
- 2 Jun 2010
Explore 3N1Q in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3N1Q contains 27 α-helices and 48 β-strands across 6 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.
Chain A: 7 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-44 | 3 | |
| β-strand | 48-49 | 2 | 5 |
| α-helix | 72-74 | 3 | |
| β-strand | 78-79 | 2 | 6 |
| β-strand | 85-87 | 3 | 5 |
| 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 | 159-169 | 11 | |
| β-strand | 173-175 | 3 | 5 |
| β-strand | 182-185 | 4 | 5 |
Chain B: 7 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-44 | 3 | |
| β-strand | 48-49 | 2 | 1 |
| α-helix | 73-76 | 4 | |
| β-strand | 78-79 | 2 | 2 |
| β-strand | 86-87 | 2 | 1 |
| 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 | 159-169 | 11 | |
| β-strand | 173-178 | 6 | 1 |
| β-strand | 181-185 | 5 | 1 |
Chain C: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 831-837 | 7 | 3 |
| β-strand | 843-848 | 6 | 3 |
| β-strand | 861-868 | 8 | 4 |
| β-strand | 878-883 | 6 | 4 |
| β-strand | 888-891 | 4 | 3 |
| α-helix | 894-895 | 2 | |
| β-strand | 899-907 | 9 | 4 |
| β-strand | 912 | 1 | 4 |
| α-helix | 913-915 | 3 | |
| α-helix | 917-918 | 2 | |
| β-strand | 919-922 | 4 | 4 |
Chain D: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 831-837 | 7 | 7 |
| β-strand | 843-848 | 6 | 7 |
| β-strand | 861-868 | 8 | 8 |
| α-helix | 874-876 | 3 | |
| β-strand | 878-883 | 6 | 8 |
| β-strand | 888-891 | 4 | 7 |
| β-strand | 899-907 | 9 | 8 |
| β-strand | 912 | 1 | 8 |
| α-helix | 914-918 | 5 | |
| β-strand | 919-922 | 4 | 8 |
Chain E: 5 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 42-44 | 3 | |
| β-strand | 48-49 | 2 | 9 |
| β-strand | 78-79 | 2 | 10 |
| β-strand | 85-87 | 3 | 9 |
| β-strand | 98-99 | 2 | 10 |
| α-helix | 101-117 | 17 | |
| β-strand | 123-127 | 5 | 9 |
| α-helix | 140-143 | 4 | |
| β-strand | 146-151 | 6 | 9 |
| α-helix | 156-158 | 3 | |
| α-helix | 159-169 | 11 | |
| β-strand | 173-178 | 6 | 9 |
| β-strand | 181-185 | 5 | 9 |
Chain F: 3 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 832-837 | 6 | 11 |
| β-strand | 843-847 | 5 | 11 |
| β-strand | 861-868 | 8 | 12 |
| α-helix | 874-876 | 3 | |
| β-strand | 878-881 | 4 | 12 |
| β-strand | 888-891 | 4 | 11 |
| α-helix | 894-895 | 2 | |
| β-strand | 899-907 | 9 | 12 |
| β-strand | 912 | 1 | 12 |
| α-helix | 913-915 | 3 | |
| β-strand | 919-922 | 4 | 12 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Desert hedgehog protein | A, B, E | protein | 170 | Homo sapiens | O43323 (AlphaFold model) |
| Cell adhesion molecule-related/down-regulated by oncogenes | C, D, F | protein | 102 | Homo sapiens | Q4KMG0 (AlphaFold model) |
Sequence of entity 1 (A, B, E), FASTA
>3N1Q_1 Desert hedgehog protein (chains A, B, E)
GSGPGPGRGPVGRRRYARKQLVPLLYKQFVPGVPERTLGASGPAEGRVARGSERFRDLVP
NYNPDIIFKDEENSGADRLMTERCKERVNALAIAVMNMWPGVRLRVTEGWDEDGHHAQDS
LHYEGRALDITTSDRDRNKYGLLARLAVEAGFDWVYYESRNHVHVSVKAD
Sequence of entity 2 (C, D, F), FASTA
>3N1Q_2 Cell adhesion molecule-related/down-regulated by oncogenes (chains C, D, F)
GSTPITGPHIAYTEAVSDTQIMLKWTYIPSSNNNTPIQGFYIYYRPTDSDNDSDYKRDVV
EGSKQWHMIGHLQPETSYDIKMQCFNEGGESEFSNVMICETK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 3 |
| CA | Calcium ion | Ca | 6 |
Primary citation
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:
- 2WFQ 1.85 Å, Crystal structure of the N-terminal signalling domain of human Dhh without calcium
- 3N1G 1.9 Å, Crystal structure of DhhN bound to BOCFn3
- 2WFR 1.95 Å, Crystal structure of the N-terminal signalling domain of human Dhh with calcium
- 2WG3 2.6 Å, Crystal structure of the complex between human hedgehog-interacting protein HIP and…
Browse structure collections
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