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Catalytic domain of human phenylalanine hydroxylase FE(II)

Analyse Catalytic domain of human phenylalanine hydroxylase FE(II) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1J8T
Type: protein
Length: 307 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: FE2
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylalanine-4-hydroxylase (EC 1.14.16.1)	protein	307	49% helix, 12% strand	P00439

Ligands and binding sites

FE2 · Fe (II) 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	695	0.74	0.80	67	FE2
2	55	0.36	0.79	12	empty

Compared structures

1J8T · Catalytic Domain of Human Phenylalanine Hydroxylase Fe(II) · 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

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 1J8T · PDBe 1J8T · UniProt P00439

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