1MMK: Phenylalanine-4-hydroxylase

Crystal structure of ternary complex of the catalytic domain of human phenylalanine hydroxylase ((FeII)) complexed with tetrahydrobiopterin and thienylalanine. Determined by X-ray diffraction at 2.0 Å resolution. Released 4 Sept 2003.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
2,748
Mol. weight
38.17 kDa
Ligands
FE2, H4B, TIH
Released
4 Sept 2003

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

Secondary structure: helices and β-sheets

1MMK contains 18 α-helices and 12 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: 18 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix118-1203
β-strand12411
α-helix126-1305
α-helix152-16716
α-helix173-1764
α-helix181-20121
β-strand20212
α-helix204-21613
β-strand22013
β-strand22313
α-helix227-23812
β-strand241-24444
α-helix251-2588
β-strand262-26544
α-helix283-2842
α-helix285-2906
α-helix291-2944
α-helix297-31014
α-helix315-32511
α-helix326-3305
β-strand333-33642
β-strand339-34242
α-helix345-3484
α-helix351-3577
β-strand363-36642
α-helix369-3724
β-strand385-38952
α-helix392-40312
β-strand411-41551
β-strand420-42451

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phenylalanine-4-hydroxylaseAprotein325Homo sapiensP00439 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1MMK_1 Phenylalanine-4-hydroxylase (chains A)
GATVHELSRDKKKDTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFA
DIAYNYRHGQPIPRVEYMEEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHED
NIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPD
ICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKA
YGAGLLSSFGELQYCLSEKPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNF
AATIPRPFSVRYDPYTQRIEVLDNT

Ligands and cofactors

IDNameFormulaCopies
FE2FE (II) ionFe1
H4B5,6,7,8-tetrahydrobiopterinC9 H15 N5 O31
TIHBETA(2-thienyl)alanineC7 H9 N O2 S1

Water and common crystallization additives (SO4) are not listed.

Primary citation

2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding. Andersen, O.A., Stokka, A.J., Flatmark, T. et al. J Mol Biol (2003) 333:747-757. DOI 10.1016/j.jmb.2003.09.004 · PubMed

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

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