Iron in PDB 3hf6: Crystal Structure of Human Tryptophan Hydroxylase Type 1 with Bound Lp-521834 and Fe

All present enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase Type 1 with Bound Lp-521834 and Fe:
1.14.16.4;

The structure of Crystal Structure of Human Tryptophan Hydroxylase Type 1 with Bound Lp-521834 and Fe, PDB code: 3hf6 was solved by L.W.Tari, R.V.Swanson, M.J.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.199, 57.893, 55.604, 90.00, 93.00, 90.00
R / Rfree (%)	18.1 / 21.7

The binding sites of Iron atom in the Crystal Structure of Human Tryptophan Hydroxylase Type 1 with Bound Lp-521834 and Fe (pdb code 3hf6). 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 Crystal Structure of Human Tryptophan Hydroxylase Type 1 with Bound Lp-521834 and Fe, PDB code: 3hf6:

Iron binding site 1 out of 1 in the Crystal Structure of Human Tryptophan Hydroxylase Type 1 with Bound Lp-521834 and Fe


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Human Tryptophan Hydroxylase Type 1 with Bound Lp-521834 and Fe within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:11.2 occ:1.00 NE2 A:HIS277 2.0 9.3 1.0 O A:HOH517 2.1 15.3 1.0 NE2 A:HIS272 2.1 12.8 1.0 OE2 A:GLU317 2.2 14.1 1.0 O A:HOH421 2.2 14.9 1.0 O A:HOH516 2.3 16.8 1.0 CD2 A:HIS277 3.0 11.2 1.0 CE1 A:HIS277 3.0 11.5 1.0 CD A:GLU317 3.1 13.2 1.0 CD2 A:HIS272 3.1 11.6 1.0 CE1 A:HIS272 3.1 11.9 1.0 OE1 A:GLU317 3.3 13.3 1.0 ND1 A:HIS277 4.1 11.3 1.0 CG A:HIS277 4.2 11.4 1.0 C9 A:LX0401 4.2 17.0 1.0 OE2 A:GLU273 4.2 17.6 1.0 ND1 A:HIS272 4.2 12.2 1.0 CG A:HIS272 4.2 12.0 1.0 CG A:GLU317 4.5 13.7 1.0 CZ A:PHE250 4.5 16.7 1.0 O A:HOH506 4.5 39.1 1.0 N14 A:LX0401 4.6 18.5 1.0 CB A:ALA332 4.7 11.8 1.0 C8 A:LX0401 4.7 15.9 1.0 OH A:TYR312 4.8 15.7 1.0 CE2 A:PHE250 4.9 16.8 1.0

G.Cianchetta, T.Stouch, W.Yu, Z.-C.Shi, L.W.Tari, R.V.Swanson, M.J.Hunter, I.D.Hoffman, Q.Liu. Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed By Co-Crystal Structures and Kinetic Analysis Curr Chem Genomics V. 4 19 2010.
ISSN: ISSN 0960-894X
PubMed: 19631532
DOI: 10.2174/1875397301004010019