Fluorine in PDB 1hwk: Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin

All present enzymatic activity of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin:
1.1.1.34;

The structure of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin, PDB code: 1hwk was solved by E.S.Istvan, J.Deisenhofer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.40 / 2.22
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	74.596, 172.724, 80.008, 90.00, 117.73, 90.00
R / Rfree (%)	21.2 / 23.5

The binding sites of Fluorine atom in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin (pdb code 1hwk). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin, PDB code: 1hwk:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin within 5.0Å range: probe atom residue distance (Å) B Occ A:F2 b:47.8 occ:1.00 F1 A:1172 0.0 47.8 1.0 C84 A:1172 1.4 45.7 1.0 C85 A:1172 2.4 45.3 1.0 C83 A:1172 2.4 45.0 1.0 NE A:ARG590 2.8 39.9 1.0 CZ A:ARG590 3.1 38.6 1.0 OG A:SER661 3.3 55.5 1.0 CG1 A:VAL683 3.3 42.6 1.0 NH2 A:ARG590 3.3 40.8 1.0 CD A:ARG590 3.4 39.1 1.0 CG2 A:VAL683 3.6 42.8 1.0 C86 A:1172 3.7 44.4 1.0 C82 A:1172 3.7 44.7 1.0 NH1 A:ARG590 4.0 38.7 1.0 CB A:SER661 4.0 52.0 1.0 CB A:VAL683 4.0 40.7 1.0 CG A:ARG590 4.1 39.5 1.0 C81 A:1172 4.2 44.9 1.0 CB A:SER684 4.2 38.0 1.0 O A:VAL683 4.3 37.7 1.0 C A:VAL683 4.3 39.5 1.0 N A:SER684 4.5 38.6 1.0 CA A:VAL683 4.8 40.5 1.0 CA A:SER684 4.8 37.2 1.0 CA A:SER661 5.0 51.5 1.0

Fluorine binding site 2 out of 4 in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:51.1 occ:1.00 F1 B:1171 0.0 51.1 1.0 C84 B:1171 1.4 50.7 1.0 C85 B:1171 2.4 49.0 1.0 C83 B:1171 2.4 51.0 1.0 NH1 B:ARG590 3.0 50.6 1.0 CD B:ARG590 3.2 48.0 1.0 OG B:SER661 3.2 56.6 1.0 CG1 B:VAL683 3.3 46.6 1.0 CZ B:ARG590 3.3 50.6 1.0 NE B:ARG590 3.4 50.0 1.0 CG2 B:VAL683 3.6 47.0 1.0 C86 B:1171 3.6 48.5 1.0 C82 B:1171 3.7 49.7 1.0 CB B:VAL683 4.0 46.1 1.0 CB B:SER661 4.1 54.5 1.0 C81 B:1171 4.2 48.4 1.0 CB B:SER684 4.2 45.1 1.0 NH2 B:ARG590 4.2 47.3 1.0 CG B:ARG590 4.3 45.1 1.0 O B:VAL683 4.3 43.3 1.0 C B:VAL683 4.3 44.2 1.0 N B:SER684 4.5 44.4 1.0 CA B:VAL683 4.8 45.0 1.0 CA B:SER684 4.8 42.7 1.0 CA B:SER661 5.0 54.0 1.0

Fluorine binding site 3 out of 4 in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin within 5.0Å range: probe atom residue distance (Å) B Occ C:F4 b:51.8 occ:1.00 F1 C:1174 0.0 51.8 1.0 C84 C:1174 1.4 49.9 1.0 C85 C:1174 2.4 49.0 1.0 C83 C:1174 2.4 49.8 1.0 NE C:ARG590 2.9 43.4 1.0 CG1 C:VAL683 3.1 44.2 1.0 CZ C:ARG590 3.2 45.3 1.0 OG C:SER661 3.3 57.9 1.0 NH2 C:ARG590 3.3 45.8 1.0 CD C:ARG590 3.6 42.9 1.0 C86 C:1174 3.6 47.3 1.0 C82 C:1174 3.7 47.0 1.0 CG2 C:VAL683 3.8 42.6 1.0 CB C:VAL683 4.0 42.2 1.0 CB C:SER661 4.0 56.8 1.0 NH1 C:ARG590 4.0 44.0 1.0 C81 C:1174 4.2 46.4 1.0 CG C:ARG590 4.2 43.4 1.0 C C:VAL683 4.3 42.6 1.0 O C:VAL683 4.3 42.0 1.0 CB C:SER684 4.4 43.0 1.0 N C:SER684 4.5 41.6 1.0 CA C:VAL683 4.8 43.1 1.0 CA C:SER684 4.9 41.0 1.0 CA C:SER661 4.9 56.8 1.0

Fluorine binding site 4 out of 4 in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Atorvastatin within 5.0Å range: probe atom residue distance (Å) B Occ D:F3 b:48.2 occ:1.00 F1 D:1173 0.0 48.2 1.0 C84 D:1173 1.3 45.4 1.0 C85 D:1173 2.4 44.3 1.0 C83 D:1173 2.4 46.8 1.0 NE D:ARG590 2.9 38.8 1.0 CG1 D:VAL683 3.2 39.2 1.0 OG D:SER661 3.2 53.0 1.0 CZ D:ARG590 3.2 41.1 1.0 NH2 D:ARG590 3.3 43.4 1.0 CD D:ARG590 3.6 39.5 1.0 C86 D:1173 3.6 44.6 1.0 C82 D:1173 3.6 44.1 1.0 CG2 D:VAL683 3.9 41.5 1.0 CB D:SER661 3.9 48.6 1.0 NH1 D:ARG590 4.1 40.2 1.0 CB D:VAL683 4.1 39.6 1.0 C81 D:1173 4.1 44.4 1.0 CG D:ARG590 4.3 37.3 1.0 C D:VAL683 4.5 41.3 1.0 O D:VAL683 4.5 40.2 1.0 CB D:SER684 4.5 40.9 1.0 N D:SER684 4.7 40.0 1.0 CA D:SER661 4.8 48.4 1.0 CA D:VAL683 4.9 40.8 1.0

E.S.Istvan, J.Deisenhofer. Structural Mechanism For Statin Inhibition of Hmg-Coa Reductase. Science V. 292 1160 2001.
ISSN: ISSN 0036-8075
PubMed: 11349148
DOI: 10.1126/SCIENCE.1059344