9T1O: Phenylalanine hydroxylase (PAH) with Belinostat

Crystal structure of phenylalanine hydroxylase (PAH) with Belinostat. Determined by X-ray diffraction at 1.94 Å resolution. Released 2 Sept 2026.

Method: X-ray diffraction
Resolution: 1.94 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,784
Mol. weight: 36.75 kDa
Ligands: 5OG, FE
Released: 2 Sept 2026

Explore 9T1O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9T1O contains 20 α-helices and 14 β-strands across 1 chain. 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: 20 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	124	1	1
α-helix	125-129	5
β-strand	135-136	2	2
α-helix	140-142	3
α-helix	152-167	16
α-helix	173-176	4
α-helix	181-201	21
β-strand	202	1	3
α-helix	204-216	13
β-strand	220	1	4
β-strand	223	1	4
α-helix	224-226	3
α-helix	227-238	12
β-strand	241-244	4	5
β-strand	248-249	2	2
α-helix	250	1
α-helix	251-258	8
β-strand	262-265	4	5
α-helix	283-285	3
α-helix	286-290	5
α-helix	291-294	4
α-helix	297-310	14
α-helix	315-325	11
α-helix	326-330	5
β-strand	333-336	4	3
β-strand	339-342	4	3
α-helix	345-348	4
α-helix	351-356	6
β-strand	363-366	4	3
α-helix	369-372	4
β-strand	385-389	5	3
α-helix	392-403	12
β-strand	411-415	5	1
β-strand	420-424	5	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phenylalanine-4-hydroxylase	A	protein	309	Homo sapiens	P00439 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9T1O_1 Phenylalanine-4-hydroxylase (chains A)
TVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPR
VEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQT
CTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSD
RSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQY
CLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDP
YTQRIEVLD

Ligands and cofactors

ID	Name	Formula	Copies
5OG	Belinostat	C15 H14 N2 O4 S	1
FE	FE (III) ion	Fe	1

Water and common crystallization additives (EDO) are not listed.

Primary citation

Variant-dependent pharmacological rescue of phenylalanine hydroxylase supports a precision therapeutic strategy for phenylketonuria. Conde-Gimenez, M., Salillas, S., Galiana-Cameo, M. et al. Biomed Pharmacother (2026) 199:119371-119371. DOI 10.1016/j.biopha.2026.119371 · 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)
5FII 1.8 Å, Structure of a human aspartate kinase, chorismate mutase and TyrA domain.
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…

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