Research workbench
Full-length human phenylalanine hydroxylase (pah) in the resting state
Analyse Full-length human phenylalanine hydroxylase (pah) in the resting state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N1K
- Type
- protein
- Length
- 1,676 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
- P00439
- Ligands
- FE, CL
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 419 | 42% helix, 16% strand | P00439 |
| B | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 420 | 44% helix, 16% strand | P00439 |
| C | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 423 | 44% helix, 17% strand | P00439 |
| D | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 414 | 43% helix, 16% strand | P00439 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 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, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 797 | 0.86 | 0.89 | 96 | CL |
| 2 | 1184 | 0.85 | 0.86 | 108 | CL |
| 3 | 430 | 0.83 | 0.91 | 50 | empty |
| 4 | 484 | 0.77 | 0.84 | 47 | empty |
| 5 | 491 | 0.76 | 0.84 | 46 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2834 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 2792 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 661 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 408 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 68 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6N1K · Full-length human phenylalanine hydroxylase (PAH) in the resting state · the same entry in another collection · chain D against D, TM-score 1.00
- P00439 · AlphaFold monomer V2.0 prediction for phenylalanine-4-hydroxylase (P00439) · a predicted model of the same protein · chain D against A, TM-score 0.97
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 6N1K · PDBe 6N1K · UniProt P00439
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