Iron in PDB 3hfb: Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Lp- 534193

All present enzymatic activity of Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Lp- 534193:
1.14.16.4;

The structure of Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Lp- 534193, PDB code: 3hfb 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 / 1.92
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.354, 58.143, 56.625, 90.00, 96.77, 90.00
R / Rfree (%)	21.4 / 28.9

The binding sites of Iron atom in the Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Lp- 534193 (pdb code 3hfb). 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 Tryoptophan Hydroxylase Type 1 with Lp- 534193, PDB code: 3hfb:

Iron binding site 1 out of 1 in the Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Lp- 534193


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 Tryoptophan Hydroxylase Type 1 with Lp- 534193 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:23.4 occ:1.00 NE2 A:HIS272 2.0 19.3 1.0 NE2 A:HIS277 2.1 19.4 1.0 OE2 A:GLU317 2.2 28.8 1.0 O A:HOH414 2.3 35.0 1.0 O A:HOH413 2.4 31.1 1.0 O A:HOH412 2.5 37.0 1.0 CD2 A:HIS272 3.0 19.3 1.0 CE1 A:HIS272 3.0 16.9 1.0 CD2 A:HIS277 3.0 19.1 1.0 CD A:GLU317 3.0 28.3 1.0 CE1 A:HIS277 3.1 18.3 1.0 OE1 A:GLU317 3.2 30.5 1.0 ND1 A:HIS272 4.1 18.8 1.0 CG A:HIS272 4.1 19.1 1.0 OE2 A:GLU273 4.2 22.0 1.0 CG A:HIS277 4.2 19.9 1.0 ND1 A:HIS277 4.2 20.0 1.0 C11 A:ML4401 4.2 34.4 1.0 O A:HOH578 4.4 47.6 1.0 CG A:GLU317 4.4 25.4 1.0 CZ A:PHE250 4.5 24.0 1.0 O A:HOH411 4.5 40.1 1.0 N18 A:ML4401 4.6 37.2 1.0 OH A:TYR312 4.6 24.4 1.0 C12 A:ML4401 4.7 33.5 1.0 CB A:ALA332 4.8 19.1 1.0 CE2 A:PHE250 4.9 23.1 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: ESSN 1875-3973
PubMed: 20556201
DOI: 10.2174/1875397301004010019