MolNFT v1 · #47838 · protein
Tetrameric human phenylalanine hydroxylase
2PAH · Protein (phenylalanine hydroxylase): “Tetrameric human phenylalanine hydroxylase”. X-ray diffraction, 1 ligand (FE), 6 pockets (best druggability 0.68). MolNFT v1 #47838 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2PAH
- Type
- protein
- Length
- 651 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (phenylalanine hydroxylase)
- EC
- 1.14.16.1
- UniProt
- P00439
- Ligands
- FE
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (phenylalanine hydroxylase) (EC 1.14.16.1) | protein | 329 | 50% helix, 11% strand | P00439 |
| B | Protein (phenylalanine hydroxylase) (EC 1.14.16.1) | protein | 322 | 51% helix, 11% strand | P00439 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 514 | 0.68 | 0.78 | 56 | empty |
| 2 | 388 | 0.66 | 0.79 | 42 | FE |
| 3 | 357 | 0.54 | 0.74 | 30 | empty |
| 4 | 123 | 0.49 | 0.80 | 25 | empty |
| 5 | 202 | 0.47 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 739 Ų buried · 3 hydrogen bonds · protein-protein
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 P00439
- Elsewhere: RCSB PDB 2PAH · PDBe 2PAH · UniProt P00439
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