Tetrameric human phenylalanine hydroxylase. Determined by X-ray diffraction at 3.1 Å resolution. Released 6 Oct 1999.
Explore 2PAH in 3D Show helices and sheets RCSB PDB PDBe
2PAH contains 36 α-helices and 24 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 | 124 | 1 | 1 |
| α-helix | 125-130 | 6 | |
| 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 | 227-237 | 11 | |
| β-strand | 241-244 | 4 | 4 |
| α-helix | 251-258 | 8 | |
| β-strand | 262-265 | 4 | 4 |
| α-helix | 283-285 | 3 | |
| α-helix | 286-290 | 5 | |
| 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 | 365-366 | 2 | 2 |
| α-helix | 369-372 | 4 | |
| β-strand | 387-389 | 3 | 2 |
| α-helix | 392-404 | 13 | |
| β-strand | 411-415 | 5 | 1 |
| β-strand | 420-424 | 5 | 1 |
| α-helix | 426-450 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 124 | 1 | 5 |
| α-helix | 125-129 | 5 | |
| α-helix | 152-167 | 16 | |
| α-helix | 173-176 | 4 | |
| α-helix | 181-201 | 21 | |
| β-strand | 202 | 1 | 6 |
| α-helix | 204-216 | 13 | |
| β-strand | 220 | 1 | 7 |
| β-strand | 223 | 1 | 7 |
| α-helix | 224-226 | 3 | |
| α-helix | 227-237 | 11 | |
| β-strand | 241-244 | 4 | 8 |
| α-helix | 251-258 | 8 | |
| β-strand | 262-265 | 4 | 8 |
| α-helix | 283-285 | 3 | |
| α-helix | 286-290 | 5 | |
| α-helix | 297-310 | 14 | |
| α-helix | 315-325 | 11 | |
| α-helix | 326-330 | 5 | |
| β-strand | 333-336 | 4 | 6 |
| β-strand | 339-342 | 4 | 6 |
| α-helix | 345-348 | 4 | |
| α-helix | 351-356 | 6 | |
| β-strand | 365-366 | 2 | 6 |
| α-helix | 369-372 | 4 | |
| β-strand | 387-389 | 3 | 6 |
| α-helix | 392-405 | 14 | |
| β-strand | 411-415 | 5 | 5 |
| β-strand | 420-424 | 5 | 5 |
| α-helix | 427-449 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (phenylalanine hydroxylase) | A, B | protein | 335 | Homo sapiens | P00439 (AlphaFold model) |
>2PAH_1 PROTEIN (PHENYLALANINE HYDROXYLASE) (chains A, B) VPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRV EYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTC TGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDR SFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYC LSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPY TQRIEVLDNTQQLKILADSINSEIGILCSALQKIK
| ID | Name | Formula | Copies |
|---|---|---|---|
| FE | FE (III) ion | Fe | 2 |
Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. Fusetti, F., Erlandsen, H., Flatmark, T. et al. J Biol Chem (1998) 273:16962-16967. DOI 10.1074/jbc.273.27.16962 · 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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