Influence of circular permutation on the folding pathway of a PDZ domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 5 Dec 2012.
Explore 4AMH in 3D Show helices and sheets RCSB PDB PDBe
4AMH contains 5 α-helices and 16 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 17-21 | 5 | 1 |
| β-strand | 28 | 1 | 2 |
| β-strand | 31 | 1 | 2 |
| β-strand | 34-39 | 6 | 1 |
| α-helix | 44-48 | 5 | |
| β-strand | 56-60 | 5 | 1 |
| β-strand | 63-64 | 2 | 1 |
| α-helix | 70-78 | 9 | |
| β-strand | 83-89 | 7 | 1 |
| β-strand | 97-103 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17-21 | 5 | 3 |
| β-strand | 28 | 1 | 4 |
| β-strand | 31 | 1 | 4 |
| β-strand | 34-39 | 6 | 3 |
| α-helix | 44-48 | 5 | |
| α-helix | 55 | 1 | |
| β-strand | 56-60 | 5 | 3 |
| β-strand | 63-64 | 2 | 3 |
| α-helix | 70-78 | 9 | |
| β-strand | 83-89 | 7 | 3 |
| β-strand | 98-103 | 6 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Disks large homolog 1 | A, B | protein | 106 | HOMO SAPIENS | Q12959 (AlphaFold model) |
>4AMH_1 DISKS LARGE HOMOLOG 1 (chains A, B) MHHHHHLVPRGSKGLGFSIAGGVGNQHWPGDNSIYVTKIIEGGAAHKDGKLQIGDKLLAV NNVALEEVTHEEAVTALKNTSDFVYLKVAKPGSGEKIMEIKLIKGP
Tolerance of Protein Folding to a Circular Permutation in a Pdz Domain. Hultqvist, G., Punekar, A.S., Morrone, A. et al. PLoS One (2012) 7:50055. DOI 10.1371/JOURNAL.PONE.0050055 · PubMed
Other PDB entries of the same protein (UniProt Q12959 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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