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Fluorine in PDB 2hnz: Crystal Structure of E138K Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2

Enzymatic activity of Crystal Structure of E138K Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2

All present enzymatic activity of Crystal Structure of E138K Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2:
2.7.7.49;

Protein crystallography data

The structure of Crystal Structure of E138K Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2, PDB code: 2hnz was solved by J.Ren, C.E.Nichols, A.Stamp, P.P.Chamberlain, D.K.Stammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.96 / 3.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 138.800, 114.900, 65.900, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 27.7

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of E138K Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2 (pdb code 2hnz). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Crystal Structure of E138K Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2, PDB code: 2hnz:

Fluorine binding site 1 out of 1 in 2hnz

Go back to Fluorine Binding Sites List in 2hnz
Fluorine binding site 1 out of 1 in the Crystal Structure of E138K Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of E138K Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F999

b:44.0
occ:1.00
F18 A:PC0999 0.0 44.0 1.0
C18 A:PC0999 1.3 51.5 1.0
C13 A:PC0999 2.4 52.4 1.0
C17 A:PC0999 2.4 50.0 1.0
O17 A:PC0999 2.8 47.3 1.0
C12 A:PC0999 2.9 49.6 1.0
N2 A:PC0999 3.3 40.8 1.0
CB A:TYR188 3.3 44.7 1.0
C3 A:PC0999 3.5 49.2 1.0
N10 A:PC0999 3.5 36.3 1.0
N14 A:PC0999 3.7 51.6 1.0
C16 A:PC0999 3.7 44.0 1.0
C11 A:PC0999 3.8 43.7 1.0
CA A:PC0999 3.8 47.6 1.0
C A:TYR188 4.1 45.3 1.0
C15 A:PC0999 4.2 45.6 1.0
CG1 A:VAL106 4.2 22.4 1.0
CG A:TYR188 4.3 47.0 1.0
O A:TYR188 4.3 47.9 1.0
CA A:TYR188 4.3 43.9 1.0
CD2 A:TYR188 4.3 41.8 1.0
N A:VAL189 4.5 43.7 1.0
C1 A:PC0999 4.5 46.3 1.0
C9 A:PC0999 4.7 53.2 1.0
CB A:PC0999 4.7 41.7 1.0
C A:VAL189 4.8 50.6 1.0
N A:GLY190 4.8 50.2 1.0
CG2 A:VAL106 4.8 47.6 1.0
C4 A:PC0999 4.8 56.9 1.0

Reference:

J.Ren, C.E.Nichols, A.Stamp, P.P.Chamberlain, R.Ferris, K.L.Weaver, S.A.Short, D.K.Stammers. Structural Insights Into Mechanisms of Non-Nucleoside Drug Resistance For Hiv-1 Reverse Transcriptases Mutated at Codons 101 or 138. Febs J. V. 273 3850 2006.
ISSN: ISSN 1742-464X
PubMed: 16911530
DOI: 10.1111/J.1742-4658.2006.05392.X
Page generated: Mon Jul 14 13:22:50 2025

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