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Chlorine in PDB 1jlc: Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2

Enzymatic activity of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2

All present enzymatic activity of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2:
2.7.7.49;

Protein crystallography data

The structure of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2, PDB code: 1jlc was solved by J.Ren, C.Nichols, L.Bird, P.Chamberlain, K.Weaver, S.Short, D.I.Stuart, D.K.Stammers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.79 / 3.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 139.200, 109.300, 73.500, 90.00, 90.00, 90.00
R / Rfree (%) 22.5 / 28.2

Other elements in 1jlc:

The structure of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2 also contains other interesting chemical elements:

Fluorine (F) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2 (pdb code 1jlc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2, PDB code: 1jlc:

Chlorine binding site 1 out of 1 in 1jlc

Go back to Chlorine Binding Sites List in 1jlc
Chlorine binding site 1 out of 1 in the Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Pett-2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl999

b:66.0
occ:1.00
 CL7 A:FTC999 0.0 66.0 1.0
C4 A:FTC999 1.7 74.3 1.0
C3 A:FTC999 2.7 74.6 1.0
C5 A:FTC999 2.7 72.2 1.0
CB A:LEU234 3.5 59.8 1.0
O A:HIS235 3.5 70.4 1.0
C A:HIS235 3.6 66.0 1.0
OH A:TYR318 3.8 49.6 1.0
C A:LEU234 3.8 61.3 1.0
N A:HIS235 3.9 58.0 1.0
O A:LEU234 3.9 60.6 1.0
N A:PRO236 4.0 66.1 1.0
N2 A:FTC999 4.0 77.8 1.0
CG2 A:VAL106 4.0 57.7 1.0
C6 A:FTC999 4.0 70.7 1.0
CA A:HIS235 4.2 61.9 1.0
CA A:LEU234 4.3 62.3 1.0
CA A:PRO236 4.3 67.7 1.0
CD2 A:PHE227 4.5 65.4 1.0
CB A:VAL106 4.5 67.8 1.0
CG1 A:VAL106 4.5 74.7 1.0
CA A:FTC999 4.5 70.9 1.0
C1 A:FTC999 4.5 76.2 1.0
CD1 A:LEU234 4.6 55.4 1.0
CG A:LEU234 4.6 64.9 1.0
CZ A:TYR318 4.7 56.6 1.0
CD A:PRO236 4.7 62.7 1.0
CG A:PRO236 4.9 69.9 1.0

Reference:

J.Ren, C.Nichols, L.Bird, P.Chamberlain, K.Weaver, S.Short, D.I.Stuart, D.K.Stammers. Structural Mechanisms of Drug Resistance For Mutations at Codons 181 and 188 in Hiv-1 Reverse Transcriptase and the Improved Resilience of Second Generation Non-Nucleoside Inhibitors. J.Mol.Biol. V. 312 795 2001.
ISSN: ISSN 0022-2836
PubMed: 11575933
DOI: 10.1006/JMBI.2001.4988
Page generated: Fri Jul 19 23:03:15 2024

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