Structure of N-terminal domain of human doublecortin. Determined by solution NMR. Released 29 Apr 2003.
Explore 1MJD in 3D Show helices and sheets RCSB PDB PDBe
1MJD contains 2 α-helices and 5 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 |
|---|---|---|---|
| β-strand | 53-59 | 7 | 1 |
| β-strand | 68-72 | 5 | 1 |
| α-helix | 80-91 | 12 | |
| β-strand | 103-106 | 4 | 1 |
| β-strand | 112-113 | 2 | 1 |
| α-helix | 116-118 | 3 | |
| β-strand | 123-128 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Doublecortin | A | protein | 113 | Homo sapiens | O43602 (AlphaFold model) |
>1MJD_1 DOUBLECORTIN (chains A) GAMDPEFALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINL PQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFKKVEYTKNVNPNWSVNV
The DCX-domain Tandems of Doublecortin and Doublecortin-like Kinase. Kim, M.H., Cierpicki, T., Derewenda, U. et al. Nat Struct Biol (2003) 10:324-333. DOI 10.1038/nsb918 · PubMed
Other PDB entries of the same protein (UniProt O43602 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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