5FII: Phenylalanine-4-hydroxylase

Structure of a human aspartate kinase, chorismate mutase and TyrA domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 30 Mar 2016.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: HOMO SAPIENS
Chains: 4
Atoms: 2,752
Mol. weight: 47.47 kDa
Ligands: PHE
Released: 30 Mar 2016

Explore 5FII in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5FII contains 17 α-helices and 16 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	35-42	8	1
α-helix	47-57	11
β-strand	62-69	8	1
β-strand	76-83	8	1
α-helix	85-90	6
α-helix	91-97	7
α-helix	98-102	5
β-strand	105-108	4	1

Chains B and C: 5 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	35-42	8	2
α-helix	47-57	11
β-strand	62-69	8	2
β-strand	76-83	8	2
α-helix	85-90	6
α-helix	91-97	7
α-helix	98-102	5
α-helix	104	1
β-strand	105-110	6	2

Chain D: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	35-42	8	2
α-helix	47-57	11
β-strand	62-69	8	2
β-strand	76-83	8	2
α-helix	85-90	6
α-helix	91-100	10
β-strand	105-110	6	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phenylalanine-4-hydroxylase	A, B, C, D	protein	102	HOMO SAPIENS	P00439 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>5FII_1 PHENYLALANINE-4-HYDROXYLASE (chains A, B, C, D)
SMGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDVNLTHIESRPSRLKKDE
YEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTV

Ligands and cofactors

ID	Name	Formula	Copies
PHE	Phenylalanine	C9 H11 N O2	4

Primary citation

Structural Basis for Ligand-Dependent Dimerization of Phenylalanine Hydroxylase Regulatory Domain. Patel, D., Kopec, J., Fitzpatrick, F. et al. Sci Rep (2016) 6:23748. DOI 10.1038/SREP23748 · PubMed

Other PDB entries of the same protein (UniProt P00439 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1J8U 1.5 Å, Catalytic Domain of Human Phenylalanine Hydroxylase Fe(II) in Complex with…
6HPO 1.67 Å, Crystallographic structure of the catalytic domain of Human Phenylalanine Hydroxylase…
1J8T 1.7 Å, Catalytic Domain of Human Phenylalanine Hydroxylase Fe(II)
9T1O 1.94 Å, Crystal structure of phenylalanine hydroxylase (PAH) with Belinostat
1DMW 2.0 Å, Crystal structure of double truncated human phenylalanine hydroxylase with bound…
1MMK 2.0 Å, Crystal structure of ternary complex of the catalytic domain of human phenylalanine…
1MMT 2.0 Å, Crystal structure of ternary complex of the catalytic domain of human phenylalanine…
1PAH 2.0 Å, Human phenylalanine hydroxylase dimer, residues 117-424
3PAH 2.0 Å, Human phenylalanine hydroxylase catalytic domain dimer with bound adrenaline inhibitor
4PAH 2.0 Å, Human phenylalanine hydroxylase catalytic domain dimer with bound nor-adrenaline inhibitor
1LRM 2.1 Å, Crystal structure of binary complex of the catalytic domain of human phenylalanine…
1TDW 2.1 Å, Crystal structure of double truncated human phenylalanine hydroxylase BH4-responsive PKU…

Browse structure collections

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