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Iron in PDB 8cjo: Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004

Enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004

All present enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004:
1.14.16.4;

Protein crystallography data

The structure of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004, PDB code: 8cjo was solved by A.Schuetz, K.Mallow, M.Nazare, E.Specker, U.Heinemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.31 / 1.87
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.218, 57.776, 69.6, 90, 109.35, 90
R / Rfree (%) 16.9 / 20.9

Other elements in 8cjo:

The structure of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004 also contains other interesting chemical elements:

Fluorine (F) 1 atom
Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004 (pdb code 8cjo). 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 1 in Complex with Inhibitor Km-06-004, PDB code: 8cjo:

Iron binding site 1 out of 1 in 8cjo

Go back to Iron Binding Sites List in 8cjo
Iron binding site 1 out of 1 in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004


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 1 in Complex with Inhibitor Km-06-004 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:17.2
occ:1.00
O A:HOH640 2.0 21.0 1.0
NAT A:UWL502 2.0 26.0 1.0
NE2 A:HIS277 2.1 19.3 1.0
NE2 A:HIS272 2.1 20.4 1.0
OE1 A:GLU317 2.2 21.7 1.0
OE2 A:GLU317 2.3 20.3 1.0
CD A:GLU317 2.6 22.8 1.0
CD2 A:HIS277 3.0 16.3 1.0
CE1 A:HIS277 3.0 17.2 1.0
CBC A:UWL502 3.1 28.4 1.0
CBB A:UWL502 3.1 25.6 1.0
CE1 A:HIS272 3.1 19.4 1.0
CD2 A:HIS272 3.2 22.2 1.0
CAO A:UWL502 3.6 22.8 1.0
CAN A:UWL502 3.6 26.0 1.0
CG A:GLU317 4.1 18.8 1.0
ND1 A:HIS277 4.2 16.2 1.0
CG A:HIS277 4.2 18.6 1.0
NBH A:UWL502 4.2 25.1 1.0
CBE A:UWL502 4.2 25.8 1.0
OE2 A:GLU273 4.2 24.4 1.0
ND1 A:HIS272 4.2 19.2 1.0
CG A:HIS272 4.3 20.9 1.0
CB A:ALA332 4.5 17.1 1.0
OH A:TYR312 4.5 22.8 1.0
CZ A:PHE250 4.6 27.7 1.0
O A:HOH612 4.9 32.1 1.0
CAQ A:UWL502 4.9 26.1 1.0

Reference:

E.Specker, R.Wesolowski, A.Schutz, S.Matthes, K.Mallow, M.Wasinska-Kalwa, L.Winkler, A.Oder, N.Alenina, D.Pleimes, J.P.Von Kries, U.Heinemann, M.Bader, M.Nazare. Structure-Based Design of Xanthine-Imidazopyridines and -Imidazothiazoles As Highly Potent and in Vivo Efficacious Tryptophan Hydroxylase Inhibitors. J.Med.Chem. V. 66 14866 2023.
ISSN: ISSN 0022-2623
PubMed: 37905925
DOI: 10.1021/ACS.JMEDCHEM.3C01454
Page generated: Fri Aug 9 21:46:03 2024

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