Atomistry » Chlorine » PDB 1i3l-1iqi » 1ikv
Atomistry »
  Chlorine »
    PDB 1i3l-1iqi »
      1ikv »

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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 1ikv:

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

Fluorine (F) 3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz, PDB code: 1ikv:

Chlorine binding site 1 out of 1 in 1ikv

Go back to Chlorine Binding Sites List in 1ikv
Chlorine binding site 1 out of 1 in the K103N Mutant Hiv-1 Reverse Transcriptase in Complex with Efivarenz


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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:Cl2000

b:32.1
occ:1.00
CL A:EFZ2000 0.0 32.1 1.0
C4 A:EFZ2000 1.3 34.5 1.0
C5 A:EFZ2000 2.4 33.4 1.0
C3 A:EFZ2000 2.4 36.4 1.0
CB A:LEU234 3.5 32.0 1.0
CD2 A:PHE227 3.5 64.0 1.0
C2 A:EFZ2000 3.7 35.4 1.0
CG1 A:VAL106 3.7 47.7 1.0
C6 A:EFZ2000 3.7 32.9 1.0
CG2 A:VAL106 3.9 45.9 1.0
C A:LEU234 3.9 35.1 1.0
O A:HIS235 3.9 40.1 1.0
O A:LEU234 3.9 35.7 1.0
C A:HIS235 4.0 38.1 1.0
N A:HIS235 4.1 35.4 1.0
CE2 A:PHE227 4.2 65.2 1.0
CG A:PHE227 4.2 62.2 1.0
C1 A:EFZ2000 4.2 32.9 1.0
OH A:TYR318 4.3 19.8 1.0
CB A:PHE227 4.3 58.6 1.0
CB A:VAL106 4.3 48.0 1.0
CA A:HIS235 4.3 36.5 1.0
CA A:LEU234 4.4 33.4 1.0
N A:PRO236 4.4 38.2 1.0
CG A:LEU234 4.5 30.2 1.0
CG A:PRO225 4.7 68.0 1.0
CB A:PRO225 4.7 67.5 1.0
CA A:PRO236 4.8 38.8 1.0

Reference:

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
Page generated: Sat Dec 12 08:37:57 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy