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

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

The structure of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Fluvastatin, PDB code: 1hwi 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)	43.77 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	74.765, 175.059, 74.838, 90.00, 118.25, 90.00
R / Rfree (%)	18.6 / 21.4

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


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 Fluvastatin within 5.0Å range: probe atom residue distance (Å) B Occ A:F2 b:34.7 occ:1.00 F1 A:1152 0.0 34.7 1.0 C84 A:1152 1.4 32.0 1.0 C85 A:1152 2.4 31.5 1.0 C83 A:1152 2.4 29.7 1.0 CG1 A:VAL683 2.8 30.6 1.0 CG2 A:VAL683 3.1 22.9 1.0 NE A:ARG590 3.2 26.7 1.0 CB A:VAL683 3.4 24.8 1.0 CZ A:ARG590 3.5 28.8 1.0 C86 A:1152 3.7 27.7 1.0 C82 A:1152 3.7 31.1 1.0 NH2 A:ARG590 3.7 27.6 1.0 C A:VAL683 3.7 23.7 1.0 CD A:ARG590 3.8 22.2 1.0 O A:VAL683 3.9 22.7 1.0 OG A:SER661 3.9 29.5 1.0 N A:SER684 3.9 19.9 1.0 CB A:SER684 3.9 21.4 1.0 C81 A:1152 4.2 28.3 1.0 CA A:VAL683 4.2 22.5 1.0 NH1 A:ARG590 4.3 26.4 1.0 CB A:SER661 4.4 23.1 1.0 CA A:SER684 4.4 16.9 1.0 CG A:ARG590 4.5 20.8 1.0 CD2 B:LEU857 4.6 24.5 1.0

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


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 Fluvastatin within 5.0Å range: probe atom residue distance (Å) B Occ B:F1 b:43.6 occ:1.00 F1 B:1151 0.0 43.6 1.0 C84 B:1151 1.4 36.5 1.0 C83 B:1151 2.4 34.7 1.0 C85 B:1151 2.4 34.2 1.0 CG1 B:VAL683 2.8 22.7 1.0 CG2 B:VAL683 3.0 20.2 1.0 NH1 B:ARG590 3.4 26.3 1.0 CB B:VAL683 3.5 17.9 1.0 C86 B:1151 3.7 32.3 1.0 C82 B:1151 3.7 33.0 1.0 CD B:ARG590 3.7 25.0 1.0 OG B:SER661 3.7 18.7 1.0 CB B:SER661 4.0 16.0 1.0 CZ B:ARG590 4.0 26.8 1.0 NE B:ARG590 4.1 29.6 1.0 C B:VAL683 4.2 18.1 1.0 C81 B:1151 4.2 27.2 1.0 O B:VAL683 4.3 19.5 1.0 N B:SER684 4.4 17.8 1.0 CA B:VAL683 4.4 17.4 1.0 CB B:SER684 4.5 19.9 1.0 CG B:ARG590 4.7 20.9 1.0 CD2 A:LEU857 4.9 16.4 1.0 CA B:SER661 4.9 19.6 1.0 CA B:SER684 4.9 16.7 1.0 NH2 B:ARG590 5.0 19.3 1.0 CG A:LEU862 5.0 41.4 1.0

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


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 Fluvastatin within 5.0Å range: probe atom residue distance (Å) B Occ C:F4 b:43.6 occ:1.00 F1 C:1154 0.0 43.6 1.0 C84 C:1154 1.4 35.1 1.0 C85 C:1154 2.4 33.5 1.0 C83 C:1154 2.4 34.2 1.0 CG1 C:VAL683 3.0 21.6 1.0 NE C:ARG590 3.2 28.3 1.0 CB C:VAL683 3.4 20.4 1.0 CZ C:ARG590 3.6 28.4 1.0 C86 C:1154 3.6 31.1 1.0 C82 C:1154 3.7 31.6 1.0 NH2 C:ARG590 3.8 27.9 1.0 C C:VAL683 3.8 21.0 1.0 CD C:ARG590 3.8 23.6 1.0 O C:VAL683 3.9 19.8 1.0 N C:SER684 3.9 20.9 1.0 CB C:SER684 3.9 19.1 1.0 OG C:SER661 4.0 25.6 1.0 C81 C:1154 4.1 28.4 1.0 CA C:VAL683 4.2 19.9 1.0 CA C:SER684 4.4 19.1 1.0 NH1 C:ARG590 4.4 24.5 1.0 CB C:SER661 4.4 22.0 1.0 CG C:ARG590 4.5 20.3 1.0 CD2 D:LEU857 4.6 20.1 1.0 CG2 C:VAL683 4.7 23.9 1.0

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


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 Fluvastatin within 5.0Å range: probe atom residue distance (Å) B Occ D:F3 b:37.9 occ:1.00 F1 D:1153 0.0 37.9 1.0 C84 D:1153 1.4 34.1 1.0 C85 D:1153 2.4 31.4 1.0 C83 D:1153 2.4 33.3 1.0 CG1 D:VAL683 3.0 26.8 1.0 NE D:ARG590 3.3 26.1 1.0 CB D:VAL683 3.4 24.2 1.0 C86 D:1153 3.6 28.4 1.0 CZ D:ARG590 3.7 28.2 1.0 C82 D:1153 3.7 29.4 1.0 C D:VAL683 3.8 22.6 1.0 NH2 D:ARG590 3.8 26.9 1.0 CD D:ARG590 3.8 25.3 1.0 N D:SER684 3.9 18.9 1.0 O D:VAL683 3.9 20.6 1.0 CB D:SER684 3.9 18.6 1.0 OG D:SER661 4.0 22.3 1.0 CA D:VAL683 4.2 22.4 1.0 C81 D:1153 4.2 25.9 1.0 CB D:SER661 4.4 18.6 1.0 CA D:SER684 4.4 18.5 1.0 NH1 D:ARG590 4.4 28.5 1.0 CG D:ARG590 4.5 19.8 1.0 CD2 C:LEU857 4.5 19.4 1.0 CG2 D:VAL683 4.7 29.4 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