UniProt P04176
Phenylalanine-4-hydroxylase (P04176)
Phenylalanine-4-hydroxylase (UniProt P04176), EC 1.14.16.1: 11 experimental structures on GenesisL1, 3 ligands bound, 60 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P04176
- Protein
- Phenylalanine-4-hydroxylase
- EC
- 1.14.16.1
- Experimental structures
- 11
- Predicted models
- 0
- Ligands
- 3
- Pockets
- 60 · 3 records with a druggable one
Structures
11 records of P04176 in the MolNFT archive: 11 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1PHZ | Structure of phosphorylated phenylalanine hydroxylase | x-ray diffraction | A | — | — |
| 1PHZ | Structure of phosphorylated phenylalanine hydroxylase | x-ray diffraction | A | — | — |
| 2PHM | Structure of phenylalanine hydroxylase dephosphorylated | x-ray diffraction | A | — | — |
| 2PHM | Structure of phenylalanine hydroxylase dephosphorylated | x-ray diffraction | A | — | — |
| 5DEN | The First Structure of a Full-Length Mammalian Phenylalanine Hydroxylase Reveals the Architecture… | x-ray diffraction | A, B, C, D | FE | 20 (best 0.87) |
| 5DEN | The first structure of a full-length mammalian phenylalanine hydroxylase reveals the architecture… | x-ray diffraction | A, B, C, D | — | — |
| 5EGQ | Structure of tetrameric rat phenylalanine hydroxylase mutant R270K, residues 25-453 | x-ray diffraction | A, B, C, D | SO4 | 20 (best 0.87) |
| 5EGQ | Structure of tetrameric rat phenylalanine hydroxylase mutant R270K, residues 25-453 | x-ray diffraction | A, B, C, D | — | — |
| 5FGJ | Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453 | x-ray diffraction | A, B, C, D | FE, MG | 20 (best 0.87) |
| 5FGJ | Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453 | x-ray diffraction | A, B, C, D | — | — |
| P04176 | AlphaFold monomer V2.0 prediction for phenylalanine-4-hydroxylase (P04176) | — | — | — |
Ligands
Elsewhere
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