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Fluorine in PDB 1hwl: Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522)

Enzymatic activity of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522)

All present enzymatic activity of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522):
1.1.1.34;

Protein crystallography data

The structure of Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522), PDB code: 1hwl 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) 43.29 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 74.432, 172.512, 79.987, 90.00, 117.36, 90.00
R / Rfree (%) 21.9 / 23.9

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522) (pdb code 1hwl). 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 Rosuvastatin (Formally Known As ZD4522), PDB code: 1hwl:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 1hwl

Go back to Fluorine Binding Sites List in 1hwl
Fluorine binding site 1 out of 4 in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522)


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 Rosuvastatin (Formally Known As ZD4522) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F2

b:52.6
occ:1.00
 F1 A:FBI2 0.0 52.6 1.0
C84 A:FBI2 1.4 51.4 1.0
C85 A:FBI2 2.4 50.9 1.0
C83 A:FBI2 2.4 50.7 1.0
NE A:ARG590 2.9 43.5 1.0
CZ A:ARG590 3.1 44.4 1.0
NH2 A:ARG590 3.4 44.9 1.0
CG1 A:VAL683 3.4 45.1 1.0
CD A:ARG590 3.5 43.0 1.0
CB A:SER684 3.5 40.5 1.0
C86 A:FBI2 3.7 49.7 1.0
C82 A:FBI2 3.7 50.1 1.0
NH1 A:ARG590 3.7 44.5 1.0
C A:VAL683 3.7 43.5 1.0
CB A:VAL683 3.7 45.3 1.0
N A:SER684 3.8 42.2 1.0
O A:VAL683 3.8 43.4 1.0
OG A:SER661 4.1 53.2 1.0
CA A:SER684 4.1 40.1 1.0
C81 A:FBI2 4.2 50.0 1.0
CG A:ARG590 4.3 42.1 1.0
CA A:VAL683 4.3 44.4 1.0
CD2 B:LEU857 4.6 49.1 1.0
OG A:SER684 4.7 39.9 1.0
CB A:SER661 4.9 52.6 1.0

Fluorine binding site 2 out of 4 in 1hwl

Go back to Fluorine Binding Sites List in 1hwl
Fluorine binding site 2 out of 4 in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522)


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 Rosuvastatin (Formally Known As ZD4522) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F1

b:54.8
occ:1.00
 F1 B:FBI1 0.0 54.8 1.0
C84 B:FBI1 1.3 54.9 1.0
C85 B:FBI1 2.4 55.1 1.0
C83 B:FBI1 2.4 55.3 1.0
NE B:ARG590 3.0 49.1 1.0
CZ B:ARG590 3.2 49.5 1.0
CG1 B:VAL683 3.4 47.5 1.0
NH2 B:ARG590 3.4 50.1 1.0
CD B:ARG590 3.5 48.1 1.0
CB B:SER684 3.5 46.5 1.0
C86 B:FBI1 3.6 54.7 1.0
C82 B:FBI1 3.7 54.6 1.0
CB B:VAL683 3.7 48.1 1.0
C B:VAL683 3.7 47.0 1.0
NH1 B:ARG590 3.8 48.8 1.0
N B:SER684 3.8 46.7 1.0
O B:VAL683 3.8 46.6 1.0
OG B:SER661 4.1 57.0 1.0
CA B:SER684 4.1 45.8 1.0
C81 B:FBI1 4.2 54.8 1.0
CA B:VAL683 4.3 47.6 1.0
CG B:ARG590 4.3 47.4 1.0
OG B:SER684 4.7 48.4 1.0
CD2 A:LEU857 4.7 56.0 1.0
CB B:SER661 4.9 56.4 1.0

Fluorine binding site 3 out of 4 in 1hwl

Go back to Fluorine Binding Sites List in 1hwl
Fluorine binding site 3 out of 4 in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522)


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 Rosuvastatin (Formally Known As ZD4522) within 5.0Å range:
probe atom residue distance (Å) B Occ
C:F4

b:53.7
occ:1.00
 F1 C:FBI4 0.0 53.7 1.0
C84 C:FBI4 1.4 52.9 1.0
C85 C:FBI4 2.4 52.5 1.0
C83 C:FBI4 2.4 52.9 1.0
NE C:ARG590 3.0 47.2 1.0
CZ C:ARG590 3.1 48.3 1.0
CB C:SER684 3.4 44.5 1.0
NH2 C:ARG590 3.5 48.5 1.0
CG1 C:VAL683 3.5 46.4 1.0
CD C:ARG590 3.5 46.5 1.0
C86 C:FBI4 3.6 52.2 1.0
C C:VAL683 3.6 45.2 1.0
N C:SER684 3.7 44.4 1.0
C82 C:FBI4 3.7 52.7 1.0
CB C:VAL683 3.7 46.5 1.0
NH1 C:ARG590 3.7 48.1 1.0
O C:VAL683 3.8 44.8 1.0
CA C:SER684 4.0 43.7 1.0
C81 C:FBI4 4.2 52.1 1.0
OG C:SER661 4.2 57.5 1.0
CA C:VAL683 4.3 46.1 1.0
CG C:ARG590 4.3 46.1 1.0
CD2 D:LEU857 4.5 48.3 1.0
OG C:SER684 4.6 45.3 1.0
CB C:SER661 5.0 57.3 1.0

Fluorine binding site 4 out of 4 in 1hwl

Go back to Fluorine Binding Sites List in 1hwl
Fluorine binding site 4 out of 4 in the Complex of the Catalytic Portion of Human Hmg-Coa Reductase with Rosuvastatin (Formally Known As ZD4522)


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 Rosuvastatin (Formally Known As ZD4522) within 5.0Å range:
probe atom residue distance (Å) B Occ
D:F3

b:53.4
occ:1.00
 F1 D:FBI3 0.0 53.4 1.0
C84 D:FBI3 1.4 52.4 1.0
C85 D:FBI3 2.4 52.3 1.0
C83 D:FBI3 2.4 52.5 1.0
NE D:ARG590 2.9 42.9 1.0
CZ D:ARG590 3.1 43.8 1.0
NH2 D:ARG590 3.4 44.5 1.0
CG1 D:VAL683 3.4 47.5 1.0
CD D:ARG590 3.4 42.4 1.0
CB D:SER684 3.5 43.7 1.0
C86 D:FBI3 3.6 51.8 1.0
C D:VAL683 3.6 45.5 1.0
C82 D:FBI3 3.7 51.8 1.0
N D:SER684 3.7 44.1 1.0
NH1 D:ARG590 3.7 43.8 1.0
CB D:VAL683 3.7 46.7 1.0
O D:VAL683 3.8 45.7 1.0
CA D:SER684 4.0 42.6 1.0
OG D:SER661 4.1 54.6 1.0
C81 D:FBI3 4.2 51.9 1.0
CG D:ARG590 4.2 40.8 1.0
CA D:VAL683 4.3 46.5 1.0
CD2 C:LEU857 4.6 50.4 1.0
OG D:SER684 4.6 43.8 1.0
CB D:SER661 4.9 53.4 1.0

Reference:

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
Page generated: Wed Jul 31 11:34:11 2024

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