Research workbench
Structure of tetrameric rat phenylalanine hydroxylase mutant R270K, residues 25-453
Analyse Structure of tetrameric rat phenylalanine hydroxylase mutant R270K, residues… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EGQ
- Type
- protein
- Length
- 1,642 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
- SO4
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 413 | 46% helix, 16% strand | P04176 |
| B | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 411 | 47% helix, 16% strand | P04176 |
| C | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 406 | 47% helix, 16% strand | P04176 |
| D | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 412 | 48% helix, 16% strand | P04176 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 984 | 0.87 | 0.89 | 103 | SO4 |
| 2 | 831 | 0.86 | 0.89 | 89 | SO4 |
| 3 | 97 | 0.75 | 0.96 | 25 | empty |
| 4 | 459 | 0.70 | 0.80 | 58 | empty |
| 5 | 61 | 0.69 | 0.97 | 26 | empty |
Interfaces
6 interfaces between chains.
- A–D · 3083 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 2839 Ų buried · 36 hydrogen bonds · protein-protein
- C–D · 798 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 560 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 159 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5EGQ · Structure of tetrameric rat phenylalanine hydroxylase mutant R270K, residues 25-453 · 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 C against A, TM-score 0.83
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 5EGQ · PDBe 5EGQ · UniProt P04176
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