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Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive pku mutant A313T.

Analyse Crystal structure of double truncated human phenylalanine hydroxylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TDW
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
FE
Pockets
2 · best druggability 0.71

Structure

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

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

Ligands and binding sites

  • FE · Fe (III) ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16050.710.7960empty
2560.370.7916empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1TDW · Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive PKU… · 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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