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

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

The structure of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Cerivastatin, PDB code: 1hwj 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)	43.50 / 2.26
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	74.616, 172.983, 80.159, 90.00, 117.35, 90.00
R / Rfree (%)	22.1 / 23.7

The binding sites of Fluorine atom in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Cerivastatin (pdb code 1hwj). 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 Cerivastatin, PDB code: 1hwj:
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 Cerivastatin


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 Cerivastatin within 5.0Å range: probe atom residue distance (Å) B Occ A:F2 b:41.6 occ:1.00 F1 A:1162 0.0 41.6 1.0 C84 A:1162 1.4 41.1 1.0 C83 A:1162 2.4 40.6 1.0 C85 A:1162 2.4 40.9 1.0 NE A:ARG590 2.8 42.2 1.0 CZ A:ARG590 2.9 42.0 1.0 NH2 A:ARG590 3.2 42.4 1.0 CG1 A:VAL683 3.3 40.2 1.0 CD A:ARG590 3.3 40.9 1.0 NH1 A:ARG590 3.6 42.9 1.0 C82 A:1162 3.6 40.9 1.0 CG2 A:VAL683 3.6 40.4 1.0 C86 A:1162 3.7 41.3 1.0 OG A:SER661 3.7 56.6 1.0 CB A:SER684 3.8 35.3 1.0 CB A:VAL683 4.0 39.8 1.0 O A:VAL683 4.0 37.6 1.0 C A:VAL683 4.1 38.1 1.0 CG A:ARG590 4.1 40.7 1.0 N A:SER684 4.2 37.1 1.0 C81 A:1162 4.2 41.1 1.0 CA A:SER684 4.4 35.4 1.0 CA A:VAL683 4.7 39.0 1.0 CB A:SER661 4.7 54.7 1.0 OG A:SER684 4.9 34.0 1.0

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


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 Cerivastatin within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:55.5 occ:1.00 F1 B:1161 0.0 55.5 1.0 C84 B:1161 1.4 54.6 1.0 C85 B:1161 2.4 53.9 1.0 C83 B:1161 2.4 54.5 1.0 NE B:ARG590 2.9 47.5 1.0 CZ B:ARG590 3.0 48.2 1.0 CG1 B:VAL683 3.2 47.7 1.0 NH2 B:ARG590 3.3 49.4 1.0 CD B:ARG590 3.4 46.5 1.0 NH1 B:ARG590 3.6 47.3 1.0 CG2 B:VAL683 3.6 47.9 1.0 CB B:SER684 3.6 44.9 1.0 C86 B:1161 3.7 52.7 1.0 C82 B:1161 3.7 52.9 1.0 OG B:SER661 3.8 60.5 1.0 CB B:VAL683 3.9 47.5 1.0 C B:VAL683 4.0 46.2 1.0 O B:VAL683 4.0 46.2 1.0 N B:SER684 4.0 45.4 1.0 C81 B:1161 4.2 52.2 1.0 CG B:ARG590 4.2 44.5 1.0 CA B:SER684 4.3 43.7 1.0 CA B:VAL683 4.6 46.8 1.0 OG B:SER684 4.8 45.3 1.0 CB B:SER661 4.8 58.7 1.0

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


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 Cerivastatin within 5.0Å range: probe atom residue distance (Å) B Occ C:F4 b:48.7 occ:1.00 F1 C:1164 0.0 48.7 1.0 C84 C:1164 1.4 47.6 1.0 C85 C:1164 2.4 47.0 1.0 C83 C:1164 2.4 47.6 1.0 NE C:ARG590 2.9 47.1 1.0 CZ C:ARG590 3.0 49.1 1.0 CG1 C:VAL683 3.2 43.1 1.0 NH2 C:ARG590 3.3 48.8 1.0 CD C:ARG590 3.4 45.5 1.0 NH1 C:ARG590 3.6 49.5 1.0 CB C:SER684 3.6 40.9 1.0 CG2 C:VAL683 3.6 42.4 1.0 C86 C:1164 3.6 46.9 1.0 C82 C:1164 3.7 47.1 1.0 C C:VAL683 3.9 42.4 1.0 CB C:VAL683 3.9 43.2 1.0 N C:SER684 4.0 41.7 1.0 O C:VAL683 4.0 42.2 1.0 OG C:SER661 4.0 62.2 1.0 C81 C:1164 4.2 46.8 1.0 CG C:ARG590 4.2 44.3 1.0 CA C:SER684 4.2 40.5 1.0 CA C:VAL683 4.5 43.4 1.0 OG C:SER684 4.8 42.6 1.0 CB C:SER661 4.9 61.0 1.0

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


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 Cerivastatin within 5.0Å range: probe atom residue distance (Å) B Occ D:F3 b:47.5 occ:1.00 F1 D:1163 0.0 47.5 1.0 C84 D:1163 1.3 46.9 1.0 C85 D:1163 2.4 46.9 1.0 C83 D:1163 2.4 47.3 1.0 NE D:ARG590 2.9 42.8 1.0 CZ D:ARG590 3.1 43.8 1.0 CG1 D:VAL683 3.1 43.0 1.0 NH2 D:ARG590 3.3 43.5 1.0 CD D:ARG590 3.4 42.8 1.0 CB D:SER684 3.6 40.8 1.0 CG2 D:VAL683 3.6 43.9 1.0 C86 D:1163 3.6 47.0 1.0 NH1 D:ARG590 3.6 44.2 1.0 C82 D:1163 3.6 46.4 1.0 CB D:VAL683 3.9 42.6 1.0 C D:VAL683 3.9 42.4 1.0 OG D:SER661 3.9 55.9 1.0 N D:SER684 3.9 41.5 1.0 O D:VAL683 4.0 42.4 1.0 C81 D:1163 4.1 46.6 1.0 CG D:ARG590 4.2 41.6 1.0 CA D:SER684 4.2 40.2 1.0 CA D:VAL683 4.5 42.9 1.0 OG D:SER684 4.8 39.7 1.0 CB D:SER661 4.9 54.8 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