MolNFT v1 · #22713 · protein
Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive pku mutant A313T.
1TDW · Phenylalanine-4-hydroxylase: “Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive pku mutant A313T.”. X-ray diffraction, 1 ligand (FE), 2 pockets (best druggability 0.71). MolNFT v1 #22713 on…
- PDB
- 1TDW
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylalanine-4-hydroxylase
- EC
- 1.14.16.1
- UniProt
- P00439
- Ligands
- FE
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 308 | 50% helix, 12% strand | P00439 |
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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 605 | 0.71 | 0.79 | 60 | empty |
| 2 | 56 | 0.37 | 0.79 | 16 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1TDW · Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive PKU… · the same entry in another collection · chain A against A, TM-score 1.00
- P00439 · AlphaFold monomer V2.0 prediction for phenylalanine-4-hydroxylase (P00439) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00439
- Elsewhere: RCSB PDB 1TDW · PDBe 1TDW · UniProt P00439
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