Fluorine in PDB 4g8r: Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1

The structure of Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1, PDB code: 4g8r was solved by J.A.Stuckey, D.A.Lawrence, S.-H.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.58 / 2.19
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	134.963, 65.504, 96.990, 90.00, 100.62, 90.00
R / Rfree (%)	17.5 / 21.5

The binding sites of Fluorine atom in the Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1 (pdb code 4g8r). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1, PDB code: 4g8r:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:F402 b:51.4 occ:0.00 F3 B:96P402 0.0 51.4 0.0 C24 B:96P402 1.3 51.4 0.0 F2 B:96P402 2.1 51.4 0.0 F1 B:96P402 2.1 51.4 0.0 C23 B:96P402 2.4 51.6 0.0 C25 B:96P402 2.8 51.8 0.0 C22 B:96P402 3.6 51.7 0.0 C19 B:96P402 4.2 51.9 0.5 CE B:MET71 4.2 38.6 1.0 O B:HOH536 4.5 31.0 1.0 CE2 B:TYR7 4.6 45.1 1.0 C21 B:96P402 4.7 51.8 0.0 OH B:TYR7 5.0 52.4 1.0 C20 B:96P402 5.0 51.9 0.0

Fluorine binding site 2 out of 6 in the Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:F402 b:51.4 occ:0.00 F1 B:96P402 0.0 51.4 0.0 C24 B:96P402 1.3 51.4 0.0 F2 B:96P402 2.1 51.4 0.0 F3 B:96P402 2.1 51.4 0.0 C23 B:96P402 2.3 51.6 0.0 C25 B:96P402 3.2 51.8 0.0 C22 B:96P402 3.2 51.7 0.0 C19 B:96P402 4.4 51.9 0.5 C21 B:96P402 4.4 51.8 0.0 OD2 B:ASP68 4.5 66.1 1.0 O B:HOH536 4.6 31.0 1.0 C20 B:96P402 5.0 51.9 0.0

Fluorine binding site 3 out of 6 in the Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:F402 b:51.4 occ:0.00 F2 B:96P402 0.0 51.4 0.0 C24 B:96P402 1.3 51.4 0.0 F1 B:96P402 2.1 51.4 0.0 F3 B:96P402 2.1 51.4 0.0 C23 B:96P402 2.4 51.6 0.0 C22 B:96P402 2.8 51.7 0.0 O B:HOH536 2.8 31.0 1.0 C25 B:96P402 3.6 51.8 0.0 OD2 B:ASP68 3.9 66.1 1.0 C21 B:96P402 4.2 51.8 0.0 C19 B:96P402 4.7 51.9 0.5 CG B:ASP68 4.8 58.3 1.0 OH B:TYR7 4.9 52.4 1.0 CB B:ASP68 4.9 42.3 1.0 C20 B:96P402 5.0 51.9 0.0 CE B:MET71 5.0 38.6 1.0

Fluorine binding site 4 out of 6 in the Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:F403 b:69.5 occ:0.00 F3 B:96P403 0.0 69.5 0.0 C24 B:96P403 1.3 69.5 0.0 F2 B:96P403 2.1 69.5 0.0 F1 B:96P403 2.1 69.5 0.0 C23 B:96P403 2.4 69.5 0.0 C25 B:96P403 3.0 69.6 0.0 C22 B:96P403 3.4 69.5 0.0 O B:HOH578 4.2 66.2 1.0 CG B:ARG118 4.2 42.4 1.0 C19 B:96P403 4.3 69.8 0.0 NE B:ARG118 4.3 68.8 1.0 O3 B:96P403 4.3 73.0 1.0 CD B:ARG76 4.6 38.0 1.0 C21 B:96P403 4.6 69.5 0.0 O11 B:96P403 4.7 64.4 1.0 NE B:ARG76 4.8 33.0 1.0 CZ B:ARG118 4.8 82.2 1.0 CB B:ARG76 4.8 28.6 1.0 CD B:ARG118 4.9 50.5 1.0 NH2 B:ARG118 4.9 67.1 1.0 C4 B:96P403 4.9 71.7 1.0 C20 B:96P403 5.0 69.6 0.0

Fluorine binding site 5 out of 6 in the Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:F403 b:69.5 occ:0.00 F1 B:96P403 0.0 69.5 0.0 C24 B:96P403 1.3 69.5 0.0 F3 B:96P403 2.1 69.5 0.0 F2 B:96P403 2.1 69.5 0.0 C23 B:96P403 2.4 69.5 0.0 C22 B:96P403 2.7 69.5 0.0 O B:HOH578 3.4 66.2 1.0 C25 B:96P403 3.6 69.6 0.0 C21 B:96P403 4.1 69.5 0.0 C19 B:96P403 4.8 69.8 0.0 C20 B:96P403 5.0 69.6 0.0

Fluorine binding site 6 out of 6 in the Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of A Novel Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1 within 5.0Å range: probe atom residue distance (Å) B Occ B:F403 b:69.5 occ:0.00 F2 B:96P403 0.0 69.5 0.0 C24 B:96P403 1.3 69.5 0.0 F3 B:96P403 2.1 69.5 0.0 F1 B:96P403 2.1 69.5 0.0 C23 B:96P403 2.4 69.5 0.0 C25 B:96P403 3.0 69.6 0.0 C22 B:96P403 3.4 69.5 0.0 CB B:LYS80 3.8 34.9 1.0 O B:HOH578 4.2 66.2 1.0 C19 B:96P403 4.3 69.8 0.0 O B:ARG76 4.3 32.5 1.0 C21 B:96P403 4.6 69.5 0.0 C B:ARG76 4.7 33.5 1.0 CB B:ARG76 4.8 28.6 1.0 C20 B:96P403 5.0 69.6 0.0

S.H.Li, A.A.Reinke, K.L.Sanders, C.D.Emal, J.C.Whisstock, J.A.Stuckey, D.A.Lawrence. Mechanistic Characterization and Crystal Structure of A Small Molecule Inactivator Bound to Plasminogen Activator Inhibitor-1. Proc.Natl.Acad.Sci.Usa V. 110 E4941 2013.
ISSN: ISSN 0027-8424
PubMed: 24297881
DOI: 10.1073/PNAS.1216499110