6N1K: Phenylalanine-4-hydroxylase

Full-length human phenylalanine hydroxylase (PAH) in the resting state. Determined by X-ray diffraction at 3.06 Å resolution. Released 22 May 2019.

Method: X-ray diffraction
Resolution: 3.06 Å
Organism: Homo sapiens
Chains: 4
Atoms: 13,689
Mol. weight: 207.49 kDa
Ligands: FE
Released: 22 May 2019

Explore 6N1K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6N1K contains 98 α-helices and 71 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: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	34-35	2	1
β-strand	36-42	7	2
α-helix	48-56	9
α-helix	62-64	3
β-strand	65-69	5	2
α-helix	70	1
β-strand	76-81	6	2
β-strand	83-84	2	1
α-helix	94-99	6
β-strand	107-109	3	2
β-strand	118	1	2
α-helix	119-120	2
β-strand	124	1	3
α-helix	125-129	5
α-helix	152-167	16
α-helix	173-176	4
α-helix	181-201	21
β-strand	202	1	4
α-helix	204-216	13
β-strand	220	1	5
β-strand	223	1	5
α-helix	227-237	11
β-strand	241-245	5	6
α-helix	248-250	3
α-helix	251-258	8
β-strand	262-266	5	6
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	332-336	5	4
β-strand	339-342	4	4
α-helix	345-348	4
α-helix	351-356	6
β-strand	363-366	4	4
α-helix	369-372	4
α-helix	382-383	2
β-strand	385-389	5	4
α-helix	392-405	14
β-strand	411-415	5	3
β-strand	420-424	5	3
α-helix	428-439	12

Chain B: 24 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	35-42	8	7
α-helix	47-57	11
α-helix	62-64	3
β-strand	65-69	5	7
β-strand	76-82	7	7
α-helix	92-100	9
β-strand	106-110	5	7
β-strand	118-119	2	7
α-helix	120	1
β-strand	124	1	8
α-helix	125-129	5
α-helix	152-167	16
α-helix	173-176	4
α-helix	181-201	21
β-strand	202	1	9
α-helix	204-216	13
β-strand	220	1	10
β-strand	223	1	10
α-helix	227-237	11
β-strand	241-244	4	11
α-helix	248-250	3
α-helix	251-259	9
β-strand	262-265	4	11
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	332-336	5	9
β-strand	339-342	4	9
α-helix	345-348	4
α-helix	353-356	4
β-strand	363-366	4	9
α-helix	369-372	4
α-helix	382-383	2
β-strand	385-389	5	9
α-helix	392-405	14
β-strand	411-415	5	8
β-strand	420-424	5	8
α-helix	428-444	17

Chain C: 26 helices, 17 β-strands

Element	Residues	Length	Sheet
β-strand	34-42	9	12
α-helix	47-56	10
α-helix	62-64	3
β-strand	65-69	5	12
α-helix	70	1
β-strand	76-84	9	12
α-helix	85-87	3
α-helix	94-100	7
β-strand	105-110	6	12
β-strand	118-119	2	12
α-helix	120	1
β-strand	124	1	13
α-helix	125-129	5
α-helix	152-167	16
α-helix	173-176	4
α-helix	181-201	21
β-strand	202	1	14
α-helix	204-216	13
β-strand	220	1	15
β-strand	223	1	15
α-helix	227-237	11
β-strand	241-245	5	16
α-helix	248-250	3
α-helix	251-259	9
β-strand	262-266	5	16
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	14
β-strand	339-342	4	14
α-helix	345-348	4
α-helix	351-356	6
β-strand	363-366	4	14
α-helix	369-372	4
α-helix	382-383	2
β-strand	385-389	5	14
α-helix	392-405	14
β-strand	411-415	5	13
β-strand	420-424	5	13
α-helix	428-445	18

Chain D: 23 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	34-42	9	17
α-helix	47-58	12
β-strand	65-69	5	17
β-strand	76-81	6	17
β-strand	83-84	2	17
α-helix	94-99	6
β-strand	106-110	5	17
β-strand	118-119	2	17
α-helix	120	1
β-strand	124	1	18
α-helix	125-129	5
α-helix	152-167	16
α-helix	173-176	4
α-helix	181-201	21
β-strand	202	1	19
α-helix	204-216	13
β-strand	220	1	20
β-strand	223	1	20
α-helix	227-238	12
β-strand	241-244	4	21
α-helix	248-250	3
α-helix	251-259	9
β-strand	262-265	4	21
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	19
β-strand	339-342	4	19
α-helix	345-348	4
α-helix	351-356	6
β-strand	363-366	4	19
α-helix	369-372	4
α-helix	382-383	2
β-strand	385-389	5	19
α-helix	392-405	14
β-strand	411-415	5	18
β-strand	420-424	5	18
α-helix	428-440	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Phenylalanine-4-hydroxylase	A, B, C, D	protein	451	Homo sapiens	P00439 (AlphaFold model)

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

>6N1K_1 Phenylalanine-4-hydroxylase (chains A, B, C, D)
STAVLENPGLGRKLSDFGQETSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDVN
LTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPWF
PRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYME
EEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGFR
LRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQ
FSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSEK
PKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQRI
EVLDNTQQLKILADSINSEIGILCSALQKIK

Ligands and cofactors

ID	Name	Formula	Copies
FE	FE (III) ion	Fe	4

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

Primary citation

Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium. Arturo, E.C., Gupta, K., Hansen, M.R. et al. J Biol Chem (2019) 294:10131-10145. DOI 10.1074/jbc.RA119.008294 · 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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