Structural basis of conformational transitions in the active site and 80 s loop in the FK506 binding protein FKBP12. Determined by X-ray diffraction at 1.2 Å resolution. Released 12 Feb 2014.
Explore 4N19 in 3D Show helices and sheets RCSB PDB PDBe
4N19 contains 4 α-helices and 8 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 | 2-8 | 7 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-29 | 9 | 1 |
| β-strand | 35-38 | 4 | 1 |
| β-strand | 46-49 | 4 | 1 |
| α-helix | 57-62 | 6 | |
| α-helix | 63-65 | 3 | |
| β-strand | 71-76 | 6 | 1 |
| α-helix | 78-80 | 3 | |
| β-strand | 87 | 1 | 2 |
| β-strand | 91 | 1 | 2 |
| β-strand | 97-106 | 10 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase FKBP1A | A | protein | 107 | Homo sapiens | P62942 (AlphaFold model) |
>4N19_1 Peptidyl-prolyl cis-trans isomerase FKBP1A (chains A) GVQVETISPGDGRTFPKRGQTVVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWE EGVAQMSVGQRAKLTISPDYAYGATGHPPIIPPHATLVFDVELLKLE
Structural basis of conformational transitions in the active site and 80's loop in the FK506-binding protein FKBP12. Mustafi, S.M., Brecher, M., Zhang, J. et al. Biochem J (2014) 458:525-536. DOI 10.1042/BJ20131429 · PubMed
Other PDB entries of the same protein (UniProt P62942 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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