X-ray Structure of the N-terminal Domain of Human Doublecortin. Determined by X-ray diffraction at 2.2 Å resolution. Released 19 Jul 2006.
Explore 2BQQ in 3D Show helices and sheets RCSB PDB PDBe
2BQQ 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 | 1 | 1 |
| α-helix | 116-118 | 3 | |
| β-strand | 124-128 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neuronal migration protein doublecortin | A | protein | 113 | HOMO SAPIENS | O43602 (AlphaFold model) |
>2BQQ_1 NEURONAL MIGRATION PROTEIN DOUBLECORTIN (chains A) GAMDPEFALSNEKKAKKVRFYRNGDRYFKGIVYAVSSDRFRSFDALLADLTRSLSDNINL PQGVRYIYTIDGSRKIGSMDELEEGESYVCSSDNFFDDVEYTKNVNPNWSVNV
The Dc-Module of Doublecortin: Dynamics, Domain Boundaries, and Functional Implications. Cierpicki, T., Kim, M.H., Cooper, D.R. et al. Proteins (2006) 64:874. DOI 10.1002/PROT.21068 · 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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