MolNFT v1 · #151498 · protein

Crystallographic structure of the catalytic domain of human phenylalanine hydroxylase (hpah CD) in complex with iron at 1.6 ångström

6HPO · Phenylalanine-4-hydroxylase: “Crystallographic structure of the catalytic domain of human phenylalanine hydroxylase (hpah CD) in complex…”. X-ray diffraction, 1 ligand (FE), 3 pockets (best druggability 0.71). MolNFT v1 #151498 on…

PDB: 6HPO
Type: protein
Length: 310 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: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phenylalanine-4-hydroxylase (EC 1.14.16.1)	protein	310	48% helix, 13% strand	P00439

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

3 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	612	0.71	0.79	61	FE
2	53	0.37	0.79	12	empty
3	72	0.29	0.73	15	empty

Compared structures

6HPO · Crystallographic structure of the catalytic domain of Human Phenylalanine Hydroxylase… · 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 6HPO · PDBe 6HPO · UniProt P00439

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