Research workbench
Structure of phosphorylated phenylalanine hydroxylase
Analyse Structure of phosphorylated phenylalanine hydroxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PHZ
- Type
- protein
- Length
- 403 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (phenylalanine hydroxylase)
- EC
- 1.14.16.1
- UniProt
- P04176
- Ligands
- FE
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (phenylalanine hydroxylase) (EC 1.14.16.1) | protein | 403 | 42% helix, 16% strand | P04176 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 440 | 0.79 | 0.87 | 46 | FE |
| 2 | 101 | 0.50 | 0.82 | 21 | empty |
| 3 | 132 | 0.44 | 0.76 | 24 | empty |
| 4 | 80 | 0.32 | 0.74 | 15 | empty |
| 5 | 60 | 0.27 | 0.73 | 16 | empty |
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P04176
- Elsewhere: RCSB PDB 1PHZ · PDBe 1PHZ · UniProt P04176
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