1KW0: Phenylalanine-4-hydroxylase

Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine. Determined by X-ray diffraction at 2.5 Å resolution. Released 28 Jan 2003.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,585
Mol. weight: 38.07 kDa
Ligands: TIH, H4B, FE2
Released: 28 Jan 2003

Explore 1KW0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KW0 contains 19 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: 19 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	124	1	1
α-helix	128-131	4
β-strand	136	1	2
α-helix	147-150	4
α-helix	152-166	15
α-helix	173-176	4
α-helix	181-201	21
β-strand	202	1	3
α-helix	204-217	14
β-strand	220	1	4
β-strand	223	1	4
α-helix	227-238	12
β-strand	241-244	4	5
β-strand	248	1	2
α-helix	251-257	7
α-helix	258-260	3
β-strand	262-265	4	5
α-helix	283-284	2
α-helix	285-290	6
α-helix	291-294	4
α-helix	297-310	14
α-helix	315-325	11
α-helix	326-330	5
β-strand	333-334	2	3
β-strand	341-342	2	3
α-helix	345-348	4
α-helix	351-357	7
β-strand	363-366	4	3
α-helix	369-372	4
β-strand	385-389	5	3
α-helix	392-403	12
β-strand	412-415	4	1
β-strand	420-423	4	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phenylalanine-4-hydroxylase	A	protein	325	Homo sapiens	P00439 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1KW0_1 Phenylalanine-4-hydroxylase (chains A)
GATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFA
DIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHED
NIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPD
ICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKA
YGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNF
AATIPRPFSVRYDPYTQRIEVLDNT

Ligands and cofactors

ID	Name	Formula	Copies
TIH	BETA(2-thienyl)alanine	C7 H9 N O2 S	1
H4B	5,6,7,8-tetrahydrobiopterin	C9 H15 N5 O3	1
FE2	FE (II) ion	Fe	1

Primary citation

Crystal Structure of the Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its Implications for the Mechanism of Catalysis and Substrate Activation. Andersen, O.A., Flatmark, T., Hough, E. J Mol Biol (2002) 320:1095-1108. DOI 10.1016/S0022-2836(02)00560-0 · 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.
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…

Browse structure collections

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