Chlorine in PDB 5juz: Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057

All present enzymatic activity of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057:
2.5.1.1; 2.5.1.10;

The structure of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057, PDB code: 5juz was solved by J.Park, A.Magder, C.Y.Leung, Y.S.Tsantrizos, A.M.Berghuis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	78.42 / 2.40
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.900, 110.900, 77.000, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 22.7

The binding sites of Chlorine atom in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057 (pdb code 5juz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057, PDB code: 5juz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057 within 5.0Å range: probe atom residue distance (Å) B Occ F:Cl401 b:90.1 occ:1.00 OD2 F:ASP80 3.2 91.8 1.0 NH1 F:ARG84 3.4 73.1 1.0 CB F:ASP80 3.4 79.7 1.0 CG F:ASP80 3.8 85.9 1.0 OD1 F:ASP78 3.8 97.9 1.0 CZ F:ARG84 4.5 72.3 1.0 O F:HOH563 4.5 63.2 1.0 CG F:ASP78 4.7 99.1 1.0 CA F:ASP80 4.8 77.6 1.0 NH2 F:ARG84 4.8 75.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Cl-06-057 within 5.0Å range: probe atom residue distance (Å) B Occ F:Cl402 b:71.0 occ:1.00 ND2 F:ASN59 3.1 61.2 1.0 O F:HOH523 3.2 36.3 1.0 O F:HOH578 3.3 57.0 1.0 N F:ASN59 3.5 52.6 1.0 CB F:ASN59 3.5 55.4 1.0 CB F:LYS57 3.6 59.6 1.0 CG F:ASN59 3.7 59.4 1.0 NH1 F:ARG60 3.7 58.4 1.0 N F:TYR58 3.7 51.8 1.0 N F:LYS57 3.9 59.1 1.0 C F:LYS57 3.9 55.8 1.0 CA F:LYS57 3.9 57.5 1.0 CA F:ASN59 4.1 52.0 1.0 CAX F:YL4403 4.1 85.9 1.0 O F:HOH516 4.3 45.5 1.0 CAL F:YL4403 4.3 92.6 1.0 CG F:LYS57 4.4 64.2 1.0 C F:TYR58 4.5 51.4 1.0 CAW F:YL4403 4.5 95.8 1.0 NAQ F:YL4403 4.6 89.8 1.0 CA F:TYR58 4.6 50.7 1.0 O F:LYS57 4.6 56.6 1.0 OD1 F:ASN59 4.7 60.4 1.0 O F:HOH582 4.7 59.8 1.0 N F:ARG60 4.8 44.3 1.0 OBC F:YL4403 4.9 0.4 1.0 CAH F:YL4403 4.9 90.2 1.0 C5 F:YL4403 5.0 96.2 1.0 C F:ASN59 5.0 48.8 1.0

J.Park, C.Y.Leung, A.N.Matralis, C.M.Lacbay, M.Tsakos, G.Fernandez De Troconiz, A.M.Berghuis, Y.S.Tsantrizos. Pharmacophore Mapping of Thienopyrimidine-Based Monophosphonate (Thp-Mp) Inhibitors of the Human Farnesyl Pyrophosphate Synthase. J. Med. Chem. V. 60 2119 2017.
ISSN: ISSN 1520-4804
PubMed: 28208018
DOI: 10.1021/ACS.JMEDCHEM.6B01888