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Human phenylalanine hydroxylase catalytic domain dimer with bound dopamine inhibitor

Analyse Human phenylalanine hydroxylase catalytic domain dimer with bound dopamine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5PAH
Type
protein
Length
308 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylalanine 4-monooxygenase
EC
1.14.16.1
UniProt
P00439
Ligands
LDP, FE
Pockets
3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenylalanine 4-monooxygenase (EC 1.14.16.1)protein30850% helix, 12% strandP00439

Ligands and binding sites

  • LDP · L-dopamine · ligand · chains A
  • FE · Fe (III) ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16190.720.7959FE, LDP
2500.360.7912empty
3680.280.7318empty

Compared structures

  • 5PAH · Human phenylalanine hydroxylase catalytic domain dimer with bound dopamine inhibitor · 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 0.99

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