MolNFT v1 · #160098 · protein

Human phenylalanine hydroxylase catalytic domain dimer with bound L- dopa (3,4-dihydroxyphenylalanine) inhibitor

6PAH · Phenylalanine 4-monooxygenase: “Human phenylalanine hydroxylase catalytic domain dimer with bound L- dopa (3,4-dihydroxyphenylalanine)…”. X-ray diffraction, 2 ligands (DAH, FE), 1 pocket (best druggability 0.72). MolNFT v1 #160098…

PDB: 6PAH
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: DAH, FE
Pockets: 1 · best druggability 0.72

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylalanine 4-monooxygenase (EC 1.14.16.1)	protein	308	49% helix, 12% strand	P00439

Ligands and binding sites

DAH · 3,4-dihydroxyphenylalanine · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	637	0.72	0.79	61	FE, DAH

Compared structures

6PAH · Human phenylalanine hydroxylase catalytic domain dimer with bound L-dopa… · 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 6PAH · PDBe 6PAH · UniProt P00439

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