Crystal Structure of the N-terminal domain of human FKBP52. Determined by X-ray diffraction at 2.4 Å resolution. Released 30 Dec 2002.
Explore 1N1A in 3D Show helices and sheets RCSB PDB PDBe
1N1A contains 7 α-helices and 18 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 | 23-24 | 2 | 1 |
| β-strand | 33-39 | 7 | 1 |
| β-strand | 52-61 | 10 | 1 |
| β-strand | 66-69 | 4 | 1 |
| β-strand | 77-80 | 4 | 1 |
| α-helix | 88-94 | 7 | |
| α-helix | 97-98 | 2 | |
| β-strand | 102-107 | 6 | 1 |
| α-helix | 109-111 | 3 | |
| β-strand | 118 | 1 | 2 |
| β-strand | 122 | 1 | 2 |
| β-strand | 128-138 | 11 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-21 | 3 | |
| β-strand | 23-24 | 2 | 3 |
| β-strand | 33-39 | 7 | 3 |
| β-strand | 52-61 | 10 | 3 |
| β-strand | 66-69 | 4 | 3 |
| β-strand | 77-80 | 4 | 3 |
| α-helix | 88-94 | 7 | |
| α-helix | 97-98 | 2 | |
| β-strand | 102-107 | 6 | 3 |
| α-helix | 109-111 | 3 | |
| β-strand | 118 | 1 | 4 |
| β-strand | 122 | 1 | 4 |
| β-strand | 128-138 | 11 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FKBP52 | A, B | protein | 140 | Homo sapiens | Q02790 (AlphaFold model) |
>1N1A_1 FKBP52 (chains A, B) MTAEEMKATESGAQSAPLPMEGVDISPKQDEGVLKVIKREGTGTEMPMIGDRVFVHYTGW LLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAIATMKVGEVCHITCKPEYAYGSAGSPP KIPPNATLVFEVELFEFKGE
Structure of the N-terminal domain of human FKBP52. Li, P., Ding, Y., Wu, B. et al. Acta Crystallogr D Biol Crystallogr (2003) 59:16-22. DOI 10.1107/S0907444902017523 · PubMed
Other PDB entries of the same protein (UniProt Q02790 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1N1A directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.