Fluorine in PDB 1ikv: K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz

All present enzymatic activity of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz:
2.7.7.49;

The structure of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz, PDB code: 1ikv was solved by J.Lindberg, T.Unge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.84 / 3.00
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	119.633, 157.168, 156.149, 90.00, 90.00, 90.00
R / Rfree (%)	22.8 / 29.4

The structure of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Fluorine atom in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz (pdb code 1ikv). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz, PDB code: 1ikv:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz within 5.0Å range: probe atom residue distance (Å) B Occ A:F2000 b:33.2 occ:1.00 F1 A:EFZ2000 0.0 33.2 1.0 C13 A:EFZ2000 1.4 33.4 1.0 F2 A:EFZ2000 2.3 34.0 1.0 F3 A:EFZ2000 2.3 31.9 1.0 C7 A:EFZ2000 2.5 34.4 1.0 C8 A:EFZ2000 2.8 35.7 1.0 C6 A:EFZ2000 3.1 32.9 1.0 CB A:TYR188 3.1 25.5 1.0 C5 A:EFZ2000 3.4 33.4 1.0 C A:TYR188 3.5 31.7 1.0 CG2 A:VAL106 3.5 45.9 1.0 C9 A:EFZ2000 3.6 36.0 1.0 O A:TYR188 3.7 31.5 1.0 O2 A:EFZ2000 3.7 35.4 1.0 N A:VAL189 3.8 31.4 1.0 CA A:TYR188 3.9 30.8 1.0 C A:VAL189 4.0 32.3 1.0 N A:GLY190 4.1 32.8 1.0 CG A:TYR188 4.2 21.9 1.0 C1 A:EFZ2000 4.3 32.9 1.0 CD2 A:TYR188 4.3 19.5 1.0 CA A:VAL189 4.3 31.8 1.0 O A:VAL189 4.3 32.1 1.0 CB A:VAL106 4.4 48.0 1.0 C14 A:EFZ2000 4.5 33.9 1.0 CA A:GLY190 4.6 34.9 1.0 C4 A:EFZ2000 4.6 34.5 1.0 C10 A:EFZ2000 4.7 35.3 1.0 N A:EFZ2000 4.8 31.9 1.0

Fluorine binding site 2 out of 3 in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz within 5.0Å range: probe atom residue distance (Å) B Occ A:F2000 b:34.0 occ:1.00 F2 A:EFZ2000 0.0 34.0 1.0 C13 A:EFZ2000 1.4 33.4 1.0 F3 A:EFZ2000 2.3 31.9 1.0 F1 A:EFZ2000 2.3 33.2 1.0 C7 A:EFZ2000 2.5 34.4 1.0 C6 A:EFZ2000 3.0 32.9 1.0 O2 A:EFZ2000 3.1 35.4 1.0 C14 A:EFZ2000 3.2 33.9 1.0 N A:EFZ2000 3.4 31.9 1.0 C1 A:EFZ2000 3.4 32.9 1.0 CA A:GLY190 3.4 34.9 1.0 N A:GLY190 3.5 32.8 1.0 CG2 A:VAL179 3.7 43.4 1.0 C8 A:EFZ2000 3.7 35.7 1.0 C5 A:EFZ2000 3.9 33.4 1.0 O1 A:EFZ2000 3.9 34.6 1.0 C A:VAL189 4.1 32.3 1.0 O A:VAL179 4.3 44.5 1.0 CG2 A:VAL106 4.3 45.9 1.0 C A:GLY190 4.3 36.2 1.0 CG1 A:VAL179 4.4 41.5 1.0 C2 A:EFZ2000 4.5 35.4 1.0 CB A:VAL106 4.5 48.0 1.0 O A:VAL189 4.6 32.1 1.0 CB A:VAL179 4.7 41.6 1.0 O A:GLY190 4.7 34.5 1.0 O A:TYR188 4.8 31.5 1.0 CA A:VAL189 4.8 31.8 1.0 C4 A:EFZ2000 4.9 34.5 1.0 C9 A:EFZ2000 4.9 36.0 1.0 C A:TYR188 5.0 31.7 1.0

Fluorine binding site 3 out of 3 in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz within 5.0Å range: probe atom residue distance (Å) B Occ A:F2000 b:31.9 occ:1.00 F3 A:EFZ2000 0.0 31.9 1.0 C13 A:EFZ2000 1.4 33.4 1.0 F2 A:EFZ2000 2.3 34.0 1.0 F1 A:EFZ2000 2.3 33.2 1.0 C7 A:EFZ2000 2.4 34.4 1.0 O2 A:EFZ2000 2.8 35.4 1.0 C8 A:EFZ2000 2.9 35.7 1.0 CG2 A:VAL179 3.1 43.4 1.0 O A:TYR188 3.5 31.5 1.0 C14 A:EFZ2000 3.6 33.9 1.0 C9 A:EFZ2000 3.8 36.0 1.0 C6 A:EFZ2000 3.8 32.9 1.0 O A:VAL179 3.9 44.5 1.0 CB A:TYR181 3.9 32.0 1.0 N A:TYR181 4.0 34.4 1.0 C A:TYR188 4.1 31.7 1.0 CB A:TYR188 4.1 25.5 1.0 O1 A:EFZ2000 4.1 34.6 1.0 C A:VAL179 4.4 42.8 1.0 N A:GLY190 4.4 32.8 1.0 N A:EFZ2000 4.5 31.9 1.0 CB A:VAL179 4.5 41.6 1.0 CA A:TYR181 4.6 33.9 1.0 C1 A:EFZ2000 4.6 32.9 1.0 N A:VAL189 4.7 31.4 1.0 C A:ILE180 4.7 36.3 1.0 C5 A:EFZ2000 4.8 33.4 1.0 CA A:TYR188 4.8 30.8 1.0 N A:ILE180 4.8 40.5 1.0 C A:VAL189 4.8 32.3 1.0 CA A:ILE180 4.8 39.0 1.0 CA A:VAL189 4.8 31.8 1.0 CG1 A:VAL179 5.0 41.5 1.0 C10 A:EFZ2000 5.0 35.3 1.0

J.Lindberg, S.Sigurdsson, S.Lowgren, H.O.Andersson, C.Sahlberg, R.Noreen, K.Fridborg, H.Zhang, T.Unge. Structural Basis For the Inhibitory Efficacy of Efavirenz (Dmp-266), MSC194 and PNU142721 Towards the Hiv-1 Rt K103N Mutant. Eur.J.Biochem. V. 269 1670 2002.
ISSN: ISSN 0014-2956
PubMed: 11895437
DOI: 10.1046/J.1432-1327.2002.02811.X