MolNFT v1 · #14858 · protein
Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (FE(II)) complexed with tetrahydrobiopterin and norleucine
1MMT · Phenylalanine-4-hydroxylase: “Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase (FE(II))…”. X-ray diffraction, 4 ligands (H4B, NLE, FE2), 4 pockets (best druggability 0.76). MolNFT v1…
- 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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