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Chlorine in PDB 1jkh: Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Dmp-266(Efavirenz)

Enzymatic activity of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Dmp-266(Efavirenz)

All present enzymatic activity of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Dmp-266(Efavirenz):
2.7.7.49;

Protein crystallography data

The structure of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Dmp-266(Efavirenz), PDB code: 1jkh 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) 29.68 / 2.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 138.500, 109.000, 73.200, 90.00, 90.00, 90.00
R / Rfree (%) 23.6 / 30.3

Other elements in 1jkh:

The structure of Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Dmp-266(Efavirenz) also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Dmp-266(Efavirenz) (pdb code 1jkh). 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 Dmp-266(Efavirenz), PDB code: 1jkh:

Chlorine binding site 1 out of 1 in 1jkh

Go back to Chlorine Binding Sites List in 1jkh
Chlorine binding site 1 out of 1 in the Crystal Structure of Y181C Mutant Hiv-1 Reverse Transcriptase in Complex with Dmp-266(Efavirenz)


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 Dmp-266(Efavirenz) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl999

b:53.9
occ:1.00
 CL A:EFZ999 0.0 53.9 1.0
C4 A:EFZ999 1.7 41.7 1.0
C5 A:EFZ999 2.7 38.1 1.0
C3 A:EFZ999 2.7 44.2 1.0
O A:HIS235 3.4 58.0 1.0
CB A:LEU234 3.6 48.5 1.0
O A:LEU234 3.7 54.7 1.0
C A:HIS235 3.8 55.7 1.0
C A:LEU234 3.8 51.5 1.0
CD2 A:PHE227 3.9 69.6 1.0
CG1 A:VAL106 4.0 43.4 1.0
C6 A:EFZ999 4.0 46.5 1.0
C2 A:EFZ999 4.0 31.3 1.0
OH A:TYR318 4.1 48.5 1.0
CG2 A:VAL106 4.1 37.8 1.0
CG A:LEU234 4.1 53.8 1.0
N A:HIS235 4.2 48.8 1.0
N A:PRO236 4.2 53.8 1.0
CA A:PRO236 4.3 49.0 1.0
CB A:VAL106 4.3 43.4 1.0
CA A:LEU234 4.3 50.6 1.0
CE2 A:PHE227 4.3 76.2 1.0
CA A:HIS235 4.4 55.0 1.0
CD2 A:LEU234 4.5 52.9 1.0
C1 A:EFZ999 4.5 42.8 1.0
CZ A:TYR318 4.9 40.7 1.0
CD A:PRO236 5.0 56.8 1.0
CG A:PHE227 5.0 61.8 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 23:03:03 2024

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