Catalytic Domain of Human Phenylalanine Hydroxylase Fe(II). Determined by X-ray diffraction at 1.7 Å resolution. Released 22 May 2002.
Explore 1J8T in 3D Show helices and sheets RCSB PDB PDBe
1J8T contains 19 α-helices and 12 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 | 124 | 1 | 1 |
| α-helix | 125-133 | 9 | |
| α-helix | 140-142 | 3 | |
| α-helix | 152-167 | 16 | |
| α-helix | 173-176 | 4 | |
| α-helix | 181-201 | 21 | |
| β-strand | 202 | 1 | 2 |
| α-helix | 204-216 | 13 | |
| β-strand | 220 | 1 | 3 |
| β-strand | 223 | 1 | 3 |
| α-helix | 224-226 | 3 | |
| α-helix | 227-238 | 12 | |
| β-strand | 241-244 | 4 | 4 |
| α-helix | 251-259 | 9 | |
| β-strand | 262-265 | 4 | 4 |
| α-helix | 283-284 | 2 | |
| α-helix | 285-290 | 6 | |
| α-helix | 291-294 | 4 | |
| α-helix | 297-310 | 14 | |
| α-helix | 315-325 | 11 | |
| α-helix | 326-330 | 5 | |
| β-strand | 333-336 | 4 | 2 |
| β-strand | 339-342 | 4 | 2 |
| α-helix | 345-348 | 4 | |
| α-helix | 351-356 | 6 | |
| β-strand | 363-366 | 4 | 2 |
| α-helix | 369-372 | 4 | |
| β-strand | 385-389 | 5 | 2 |
| α-helix | 392-403 | 12 | |
| β-strand | 412-415 | 4 | 1 |
| β-strand | 420-423 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phenylalanine-4-hydroxylase | A | protein | 325 | Homo sapiens | P00439 (AlphaFold model) |
>1J8T_1 PHENYLALANINE-4-HYDROXYLASE (chains A) GATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFA DIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHED NIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPD ICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKA YGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNF AATIPRPFSVRYDPYTQRIEVLDNT
| ID | Name | Formula | Copies |
|---|---|---|---|
| FE2 | FE (II) ion | Fe | 1 |
High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin. Andersen, O.A., Flatmark, T., Hough, E. J Mol Biol (2001) 314:279-291. DOI 10.1006/jmbi.2001.5061 · PubMed
Other PDB entries of the same protein (UniProt P00439 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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