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Human phenylalanine hydroxylase catalytic domain dimer with bound nor- adrenaline inhibitor

Analyse Human phenylalanine hydroxylase catalytic domain dimer with bound nor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4PAH
Type
protein
Length
308 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phenylalanine hydroxylase
EC
1.14.16.1
UniProt
P00439
Ligands
LNR, FE
Pockets
1 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APhenylalanine hydroxylase (EC 1.14.16.1)protein30850% helix, 13% strandP00439

Ligands and binding sites

  • LNR · L-norepinephrine · 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16050.710.7959FE, LNR

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 4PAH · Human phenylalanine hydroxylase catalytic domain dimer with bound nor-adrenaline 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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