MolNFT v1 · #116470 · protein
The first structure of a full-length mammalian phenylalanine hydroxylase reveals the architecture of an auto-inhibited tetramer
5DEN · Phenylalanine-4-hydroxylase: “The first structure of a full-length mammalian phenylalanine hydroxylase reveals the architecture of an…”. X-ray diffraction, 1 ligand (FE), 20 pockets (best druggability 0.87). MolNFT v1 #116470 on…
- PDB
- 5DEN
- Type
- protein
- Length
- 1,688 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylalanine-4-hydroxylase
- EC
- 1.14.16.1
- UniProt
- P04176
- Ligands
- FE
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 423 | 45% helix, 15% strand | P04176 |
| B | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 420 | 45% helix, 15% strand | P04176 |
| C | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 421 | 45% helix, 15% strand | P04176 |
| D | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 424 | 45% helix, 15% strand | P04176 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 871 | 0.87 | 0.89 | 92 | empty |
| 2 | 791 | 0.86 | 0.89 | 74 | empty |
| 3 | 525 | 0.76 | 0.83 | 64 | FE |
| 4 | 483 | 0.75 | 0.84 | 49 | FE |
| 5 | 440 | 0.75 | 0.84 | 49 | FE |
Interfaces
6 interfaces between chains.
- A–C · 2943 Ų buried · 31 hydrogen bonds · protein-protein
- B–D · 2898 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 794 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 423 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 143 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 5DEN · The First Structure of a Full-Length Mammalian Phenylalanine Hydroxylase Reveals the… · the same entry in another collection · chain D against D, TM-score 1.00
- P04176 · AlphaFold monomer V2.0 prediction for phenylalanine-4-hydroxylase (P04176) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 5DEN · PDBe 5DEN · UniProt P04176
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.