Iron in PDB 1toh: Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat

All present enzymatic activity of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat:
1.14.16.2;

The structure of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat, PDB code: 1toh was solved by K.E.Goodwill, C.Sabatier, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.00 / 2.30
Space group	F 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	189.323, 148.335, 57.975, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 26.8

The binding sites of Iron atom in the Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat (pdb code 1toh). 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 Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat, PDB code: 1toh:

Iron binding site 1 out of 1 in the Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Tyrosine Hydroxylase Catalytic and Tetramerization Domains From Rat within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:39.8 occ:1.00 OE2 A:GLU376 2.0 43.4 1.0 NE2 A:HIS331 2.2 45.1 1.0 O A:HOH602 2.3 45.2 1.0 NE2 A:HIS336 2.4 33.0 1.0 O A:HOH601 2.4 56.7 1.0 OE1 A:GLU376 2.6 47.0 1.0 CD A:GLU376 2.6 43.5 1.0 O A:HOH772 3.1 84.2 1.0 CD2 A:HIS331 3.2 42.2 1.0 CE1 A:HIS331 3.2 41.1 1.0 CE1 A:HIS336 3.3 35.5 1.0 CD2 A:HIS336 3.3 33.8 1.0 CG A:GLU376 4.1 41.4 1.0 O A:HOH604 4.3 56.2 1.0 ND1 A:HIS331 4.3 40.2 1.0 CG A:HIS331 4.3 43.5 1.0 ND1 A:HIS336 4.4 31.2 1.0 CG A:HIS336 4.5 29.1 1.0 OE1 A:GLU332 4.5 37.1 1.0 CB A:ALA391 4.7 32.3 1.0 CB A:PRO327 4.7 57.0 1.0

K.E.Goodwill, C.Sabatier, C.Marks, R.Raag, P.F.Fitzpatrick, R.C.Stevens. Crystal Structure of Tyrosine Hydroxylase at 2.3 A and Its Implications For Inherited Neurodegenerative Diseases. Nat.Struct.Biol. V. 4 578 1997.
ISSN: ISSN 1072-8368
PubMed: 9228951
DOI: 10.1038/NSB0797-578