Chlorine in PDB 3hhd: Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design.

All present enzymatic activity of Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design.:
2.3.1.85;

The structure of Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design., PDB code: 3hhd was solved by G.M.Pappenberger, J.Benz, R.Thoma, M.G.Rudolph, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.64 / 2.15
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	86.620, 91.160, 132.110, 73.84, 86.83, 62.54
R / Rfree (%)	16.9 / 21.1

The binding sites of Chlorine atom in the Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design. (pdb code 3hhd). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design., PDB code: 3hhd:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design. within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl964 b:76.9 occ:1.00 O C:TYR589 3.5 19.3 1.0 O C:HOH1249 4.4 26.0 1.0 O C:ALA590 4.4 28.0 1.0 CE2 C:TYR589 4.5 17.1 1.0 OG C:SER568 4.5 30.4 1.0 CZ C:TYR589 4.6 18.5 1.0 C C:TYR589 4.6 20.4 1.0 CA C:ALA590 4.7 20.0 1.0 C C:ALA590 4.7 29.6 1.0 CG2 C:ILE564 4.8 18.3 1.0 OH C:TYR589 4.9 20.5 1.0 CD2 C:TYR589 4.9 17.4 1.0 O C:HOH1731 4.9 57.5 1.0 CE1 C:TYR589 5.0 18.4 1.0

Chlorine binding site 2 out of 2 in the Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design. within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl964 b:66.2 occ:1.00 O D:HOH1539 2.7 46.6 1.0 O D:TYR589 3.8 30.4 1.0 OG D:SER568 4.2 31.8 1.0 CE2 D:TYR589 4.3 20.7 1.0 CZ D:TYR589 4.3 26.0 1.0 CG2 D:ILE564 4.5 22.9 1.0 OH D:TYR589 4.6 25.6 1.0 O D:HOH1273 4.6 26.7 1.0 CD2 D:TYR589 4.7 19.7 1.0 O D:ALA590 4.7 30.0 1.0 C D:TYR589 4.8 27.5 1.0 CA D:ALA590 4.8 24.1 1.0 CE1 D:TYR589 4.8 17.8 1.0

G.Pappenberger, J.Benz, B.Gsell, M.Hennig, A.Ruf, M.Stihle, R.Thoma, M.G.Rudolph. Structure of the Human Fatty Acid Synthase Ks-Mat Didomain As A Framework For Inhibitor Design. J.Mol.Biol. V. 397 508 2010.
ISSN: ISSN 0022-2836
PubMed: 20132826
DOI: 10.1016/J.JMB.2010.01.066