Chlorine in PDB 1hpz: Human Immunodeficiency Virus Type 1

All present enzymatic activity of Human Immunodeficiency Virus Type 1:
2.7.7.49;

The structure of Human Immunodeficiency Virus Type 1, PDB code: 1hpz was solved by J.Ding, Y.Hsiou, E.Arnold, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 3.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	223.100, 69.000, 104.000, 90.00, 106.80, 90.00
R / Rfree (%)	25.4 / 34.3

The binding sites of Chlorine atom in the Human Immunodeficiency Virus Type 1 (pdb code 1hpz). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Immunodeficiency Virus Type 1, PDB code: 1hpz:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Immunodeficiency Virus Type 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Immunodeficiency Virus Type 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl561 b:33.2 occ:1.00 CL2 A:AAP561 0.0 33.2 1.0 C2 A:AAP561 1.9 41.5 1.0 O A:AAP561 2.7 66.8 1.0 C3 A:AAP561 2.8 46.2 1.0 C1 A:AAP561 2.9 49.6 1.0 CA A:AAP561 3.4 65.0 1.0 N' A:AAP561 3.4 70.9 1.0 C A:AAP561 3.4 67.2 1.0 O A:LYS101 3.9 76.0 1.0 O' A:AAP561 3.9 87.6 1.0 CD1 A:LEU100 3.9 63.1 1.0 C4 A:AAP561 4.1 52.5 1.0 CD2 A:LEU100 4.1 70.3 1.0 C6 A:AAP561 4.2 43.0 1.0 CB A:LEU100 4.2 70.2 1.0 CG1 A:VAL179 4.3 70.3 1.0 CG A:LEU100 4.3 66.0 1.0 C1' A:AAP561 4.5 75.8 1.0 ND2 A:ASN103 4.5 94.1 1.0 N A:LYS101 4.6 83.0 1.0 C5 A:AAP561 4.7 52.5 1.0 N A:AAP561 4.8 70.1 1.0 C' A:AAP561 4.8 86.6 1.0 CG A:ASN103 4.8 90.7 1.0 CB A:VAL179 4.9 61.6 1.0 C A:LYS101 4.9 80.3 1.0

Chlorine binding site 2 out of 2 in the Human Immunodeficiency Virus Type 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Immunodeficiency Virus Type 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl561 b:24.7 occ:1.00 CL6 A:AAP561 0.0 24.7 1.0 C6 A:AAP561 1.9 43.0 1.0 C5 A:AAP561 2.8 52.5 1.0 C1 A:AAP561 2.9 49.6 1.0 CD2 A:TYR188 3.0 64.5 1.0 CA A:AAP561 3.1 65.0 1.0 C6' A:AAP561 3.5 71.6 1.0 CG1 A:VAL106 3.8 50.4 1.0 CG A:TYR188 3.9 62.4 1.0 CB A:TYR188 3.9 51.4 1.0 CE2 A:TYR188 3.9 70.1 1.0 N' A:AAP561 4.1 70.9 1.0 CD1 A:LEU234 4.1 88.7 1.0 CD2 A:PHE227 4.2 56.3 1.0 C4 A:AAP561 4.2 52.5 1.0 C A:AAP561 4.2 67.2 1.0 C2 A:AAP561 4.2 41.5 1.0 C1' A:AAP561 4.3 75.8 1.0 CE2 A:PHE227 4.4 58.8 1.0 N A:AAP561 4.5 70.1 1.0 C5' A:AAP561 4.6 70.9 1.0 CM5 A:AAP561 4.6 69.5 1.0 CB A:LEU234 4.7 83.5 1.0 C3 A:AAP561 4.7 46.2 1.0 CB A:VAL106 4.8 57.6 1.0 CA A:TYR188 4.9 47.6 1.0 CG2 A:VAL108 4.9 37.8 1.0 CG A:LEU234 5.0 85.5 1.0 CG A:PHE227 5.0 57.1 1.0

Y.Hsiou, J.Ding, K.Das, A.D.Clark Jr., P.L.Boyer, P.Lewi, P.A.Janssen, J.P.Kleim, M.Rosner, S.H.Hughes, E.Arnold. The LYS103ASN Mutation of Hiv-1 Rt: A Novel Mechanism of Drug Resistance. J.Mol.Biol. V. 309 437 2001.
ISSN: ISSN 0022-2836
PubMed: 11371163
DOI: 10.1006/JMBI.2001.4648