Solution Structure of human FK506 binding Protein 25. Determined by solution NMR. Released 20 May 2015.
Explore 2MPH in 3D Show helices and sheets RCSB PDB PDBe
2MPH contains 12 α-helices and 10 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 |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| α-helix | 12-15 | 4 | |
| α-helix | 22-32 | 11 | |
| β-strand | 33 | 1 | 1 |
| α-helix | 35-41 | 7 | |
| α-helix | 47-53 | 7 | |
| α-helix | 56-68 | 13 | |
| β-strand | 72 | 1 | 1 |
| β-strand | 111-117 | 7 | 2 |
| α-helix | 124-126 | 3 | |
| β-strand | 132-138 | 7 | 2 |
| β-strand | 144-147 | 4 | 2 |
| α-helix | 150-152 | 3 | |
| α-helix | 161 | 1 | |
| β-strand | 162-163 | 2 | 2 |
| α-helix | 173-179 | 7 | |
| β-strand | 187-192 | 6 | 2 |
| α-helix | 194-196 | 3 | |
| β-strand | 203 | 1 | 3 |
| α-helix | 204-206 | 3 | |
| β-strand | 208 | 1 | 3 |
| β-strand | 214-222 | 9 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase FKBP3 | A | protein | 224 | Homo sapiens | Q00688 (AlphaFold model) |
>2MPH_1 Peptidyl-prolyl cis-trans isomerase FKBP3 (chains A) MAAAVPQRAWTVEQLRSEQLPKKDIIKFLQEHGSDSFLAEHKLLGNIKNVAKTANKDHLV TAYNHLFETKRFKGTESISKVSEQVKNVKLNEDKPKETKSEETLDEGPPKYTKSVLKKGD KTNFPKKGDVVHCWYTGTLQDGTVFDTNIQTSAKKKKNAKPLSFKVGVGKVIRGWDEALL TMSKGEKARLEIEPEWAYGKKGQPDAKIPPNAKLTFEVELVDID
Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin. Prakash, A., Shin, J., Rajan, S. et al. Nucleic Acids Res (2016) 44:2909-2925. DOI 10.1093/nar/gkw001 · PubMed
Other PDB entries of the same protein (UniProt Q00688 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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