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Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase ((feii)) complexed with tetrahydrobiopterin and thienylalanine

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
1MMK
Type
protein
Length
309 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, TIH, FE2, SO4
Pockets
4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenylalanine-4-hydroxylase (EC 1.14.16.1)protein30947% helix, 13% strandP00439

Ligands and binding sites

  • H4B · 5,6,7,8-tetrahydrobiopterin · ligand · chains A
  • TIH · Beta(2-thienyl)alanine · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12150.770.9140FE2, H4B, TIH
2650.440.8320empty
31040.370.7516empty
4610.340.7713empty

Compared structures

  • 1MMK · 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

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