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Structure of phenylalanine hydroxylase dephosphorylated

Analyse Structure of phenylalanine hydroxylase dephosphorylated in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PHM
Type: protein
Length: 403 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (phenylalanine-4-hydroxylase)
EC: 1.14.16.1
UniProt: P04176
Ligands: FE
Pockets: 5 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (phenylalanine-4-hydroxylase) (EC 1.14.16.1)	protein	403	43% helix, 16% strand	P04176

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

5 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	429	0.76	0.85	42	FE
2	92	0.46	0.81	17	empty
3	170	0.43	0.74	27	empty
4	128	0.41	0.75	21	empty
5	50	0.28	0.75	12	empty

Compared structures

2PHM · Structure of phenylalanine hydroxylase dephosphorylated · the same entry in another collection · chain A against A, TM-score 1.00
P04176 · AlphaFold monomer V2.0 prediction for phenylalanine-4-hydroxylase (P04176) · a predicted model of the same protein · chain A against A, TM-score 0.77

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 P04176
Elsewhere: RCSB PDB 2PHM · PDBe 2PHM · UniProt P04176

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