Chlorine in PDB 5jv2: Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Mit-01-055

All present enzymatic activity of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Mit-01-055:
2.5.1.1; 2.5.1.10;

The structure of Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Mit-01-055, PDB code: 5jv2 was solved by J.Park, A.Magder, M.Tsakos, 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)	55.21 / 2.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	110.410, 110.410, 76.270, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 23.7

The binding sites of Chlorine atom in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Mit-01-055 (pdb code 5jv2). 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 Mit-01-055, PDB code: 5jv2:
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 Mit-01-055


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 Mit-01-055 within 5.0Å range: probe atom residue distance (Å) B Occ F:Cl402 b:88.3 occ:1.00 OD2 F:ASP80 3.7 76.7 1.0 OD2 F:ASP78 3.7 91.6 1.0 CB F:ASP80 3.9 68.4 1.0 NH1 F:ARG84 4.0 58.2 1.0 NH2 F:ARG84 4.2 58.2 1.0 CG F:ASP80 4.3 74.9 1.0 CZ F:ARG84 4.6 57.2 1.0 CG F:ASP78 4.6 85.8 1.0 OD1 F:ASP78 4.8 79.9 1.0 O F:HOH599 4.9 65.2 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of Human Fpps in Complex with An Allosteric Inhibitor Mit-01-055


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 Mit-01-055 within 5.0Å range: probe atom residue distance (Å) B Occ F:Cl403 b:82.2 occ:1.00 N F:ILE116 3.1 54.0 1.0 CA F:GLN115 3.5 60.4 1.0 CB F:GLN115 3.5 65.0 1.0 CG1 F:ILE116 3.8 54.7 1.0 C F:GLN115 3.8 55.3 1.0 CD1 F:ILE116 4.0 57.3 1.0 CB F:ILE116 4.0 50.0 1.0 CA F:ILE116 4.1 50.5 1.0 OH F:TYR51 4.2 54.2 1.0 CG F:GLN115 4.5 68.6 1.0 O F:GLY114 4.7 76.2 1.0 NE2 F:GLN115 4.8 78.3 1.0 N F:GLN115 4.8 62.4 1.0 O F:GLN115 5.0 51.4 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