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Structure of a human aspartate kinase, chorismate mutase and tyra domain.
Analyse Structure of a human aspartate kinase, chorismate mutase and tyra domain. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FII
- Type
- protein
- Length
- 308 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
- PHE
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 3 distinct chains · 38% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 76 | 38% helix, 37% strand | P00439 |
| B, D | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 78 | 37% helix, 38% strand | P00439 |
| C | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 76 | 38% helix, 39% strand | P00439 |
Ligands and binding sites
- PHE · Phenylalanine · ligand · 4 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 72 | 0.75 | 0.98 | 21 | PHE |
| 2 | 70 | 0.74 | 0.98 | 21 | PHE |
| 3 | 70 | 0.74 | 0.98 | 21 | PHE |
| 4 | 68 | 0.73 | 0.98 | 21 | PHE |
| 5 | 75 | 0.47 | 0.82 | 15 | empty |
Interfaces
4 interfaces between chains.
- B–D · 833 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 808 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 390 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 11 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5FII · Structure of a human aspartate kinase, chorismate mutase and TyrA domain. · 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 C against A, TM-score 0.89
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 5FII · PDBe 5FII · UniProt P00439
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