Iron in PDB 8r2s: Heme-Dependent L-Tyrosine Hydroxylase (Tyrh) From Streptomyces Sclerotialus: Fourfold Mutant

The structure of Heme-Dependent L-Tyrosine Hydroxylase (Tyrh) From Streptomyces Sclerotialus: Fourfold Mutant, PDB code: 8r2s was solved by D.Carraretto, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	78.45 / 2.70
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.61, 74.834, 156.906, 90, 90, 90
R / Rfree (%)	20.8 / 28.7

The binding sites of Iron atom in the Heme-Dependent L-Tyrosine Hydroxylase (Tyrh) From Streptomyces Sclerotialus: Fourfold Mutant (pdb code 8r2s). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Heme-Dependent L-Tyrosine Hydroxylase (Tyrh) From Streptomyces Sclerotialus: Fourfold Mutant, PDB code: 8r2s:

Iron binding site 1 out of 1 in the Heme-Dependent L-Tyrosine Hydroxylase (Tyrh) From Streptomyces Sclerotialus: Fourfold Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Heme-Dependent L-Tyrosine Hydroxylase (Tyrh) From Streptomyces Sclerotialus: Fourfold Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:137.2 occ:1.00 FE A:HEM401 0.0 137.2 1.0 ND A:HEM401 1.9 138.2 1.0 NA A:HEM401 2.0 115.8 1.0 NC A:HEM401 2.1 121.7 1.0 NB A:HEM401 2.1 115.0 1.0 C4D A:HEM401 2.8 130.3 1.0 C1D A:HEM401 2.9 133.2 1.0 C1A A:HEM401 2.9 109.8 1.0 C4A A:HEM401 3.0 98.8 1.0 NE2 A:HIS196 3.0 38.9 1.0 C4C A:HEM401 3.0 116.6 1.0 C1B A:HEM401 3.0 105.5 1.0 C1C A:HEM401 3.1 104.0 1.0 C4B A:HEM401 3.1 98.5 1.0 CHA A:HEM401 3.3 110.2 1.0 CHD A:HEM401 3.3 125.9 1.0 C4 A:IND402 3.4 76.9 1.0 CHB A:HEM401 3.4 99.4 1.0 CHC A:HEM401 3.6 95.1 1.0 CE1 A:HIS196 3.8 41.4 1.0 C9 A:IND402 3.9 79.5 1.0 C2A A:HEM401 4.0 97.2 1.0 C3A A:HEM401 4.0 89.5 1.0 CD2 A:HIS196 4.1 40.9 1.0 C3D A:HEM401 4.1 130.9 1.0 C2D A:HEM401 4.1 129.0 1.0 C3 A:IND402 4.1 82.9 1.0 C3C A:HEM401 4.2 98.4 1.0 C5 A:IND402 4.2 69.8 1.0 C2C A:HEM401 4.2 94.0 1.0 C2B A:HEM401 4.2 106.3 1.0 C3B A:HEM401 4.3 95.8 1.0 ND1 A:HIS196 5.0 41.2 1.0

D.Carraretto, L.Alonso-Cotchico, C.Martin, M.Trajkovic, H.L.Van Beek, A.Mattevi, M.W.Fraaije, M.F.Lucas, N.Loncar. Broadening the Catalytic Scope of the Peroxygenase Activity of A Bacterial Tyrosine Hydroxylase Chemcatchem 2024.
ISSN: ESSN 1867-3899
DOI: 10.1002/CCTC.202401819