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Iron in PDB 3hf8: Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Bound Lp-533401 and Fe

Enzymatic activity of Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Bound Lp-533401 and Fe

All present enzymatic activity of Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Bound Lp-533401 and Fe:
1.14.16.4;

Protein crystallography data

The structure of Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Bound Lp-533401 and Fe, PDB code: 3hf8 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 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.278, 58.238, 56.554, 90.00, 97.15, 90.00
R / Rfree (%) 19.7 / 24.1

Other elements in 3hf8:

The structure of Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Bound Lp-533401 and Fe also contains other interesting chemical elements:

Fluorine (F) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Bound Lp-533401 and Fe (pdb code 3hf8). 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 Bound Lp-533401 and Fe, PDB code: 3hf8:

Iron binding site 1 out of 1 in 3hf8

Go back to Iron Binding Sites List in 3hf8
Iron binding site 1 out of 1 in the Crystal Structure of Human Tryoptophan Hydroxylase Type 1 with Bound Lp-533401 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 Tryoptophan Hydroxylase Type 1 with Bound Lp-533401 and Fe within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:19.2
occ:1.00
 NE2 A:HIS277 2.0 15.8 1.0
O A:HOH404 2.1 31.8 1.0
NE2 A:HIS272 2.1 17.3 1.0
O A:HOH402 2.2 26.7 1.0
OE1 A:GLU317 2.2 21.5 1.0
OE2 A:GLU317 2.3 19.7 1.0
CD A:GLU317 2.6 20.6 1.0
CD2 A:HIS277 3.0 16.1 1.0
CD2 A:HIS272 3.1 17.3 1.0
CE1 A:HIS277 3.1 16.9 1.0
CE1 A:HIS272 3.1 17.3 1.0
O A:HOH403 3.7 48.3 1.0
CG A:GLU317 4.1 20.1 1.0
C32 A:ML0401 4.1 29.3 1.0
CG A:HIS277 4.1 17.4 1.0
ND1 A:HIS277 4.1 16.7 1.0
OE2 A:GLU273 4.2 20.4 1.0
ND1 A:HIS272 4.2 17.3 1.0
CG A:HIS272 4.2 18.5 1.0
N23 A:ML0401 4.3 31.9 1.0
OH A:TYR312 4.4 22.9 1.0
CZ A:PHE250 4.6 20.5 1.0
CB A:ALA332 4.6 19.0 1.0
C31 A:ML0401 4.7 28.0 1.0
N26 A:ML0401 4.8 31.8 1.0
O A:HOH833 4.8 56.1 1.0
CE2 A:PHE250 4.9 20.4 1.0
C27 A:ML0401 5.0 30.6 1.0

Reference:

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
Page generated: Sun Aug 4 11:28:57 2024

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