Research workbench
Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (FE(II)) complexed with tetrahydrobiopterin and norleucine
Analyse Crystal structure of ternary complex of the catalytic domain of human… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MMT
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylalanine-4-hydroxylase
- EC
- 1.14.16.1
- UniProt
- P00439
- Ligands
- H4B, NLE, FE2, SO4
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine-4-hydroxylase (EC 1.14.16.1) | protein | 308 | 48% helix, 13% strand | P00439 |
Ligands and binding sites
- H4B · 5,6,7,8-tetrahydrobiopterin · ligand · chains A
- NLE · Norleucine · ligand · chains A
- FE2 · Fe (II) ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.76 | 0.91 | 40 | FE2, H4B, NLE |
| 2 | 57 | 0.44 | 0.84 | 20 | empty |
| 3 | 57 | 0.40 | 0.81 | 16 | empty |
| 4 | 105 | 0.38 | 0.75 | 16 | empty |
Compared structures
- 1MMT · Crystal structure of ternary complex of the catalytic domain of human phenylalanine… · the same entry in another collection · chain A against A, TM-score 1.00
- P00439 · AlphaFold monomer V2.0 prediction for phenylalanine-4-hydroxylase (P00439) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 1MMT · PDBe 1MMT · UniProt P00439
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