Arsenic in PDB 1bhl: Cacodylated Catalytic Domain of Hiv-1 Integrase

All present enzymatic activity of Cacodylated Catalytic Domain of Hiv-1 Integrase:
2.7.7.49;

The structure of Cacodylated Catalytic Domain of Hiv-1 Integrase, PDB code: 1bhl was solved by S.Maignan, J.P.Guilloteau, Q.Zhou-Liu, C.Clement-Mella, V.Mikol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.20
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	72.500, 72.500, 65.800, 90.00, 90.00, 120.00
R / Rfree (%)	22.4 / 26.4

The binding sites of Arsenic atom in the Cacodylated Catalytic Domain of Hiv-1 Integrase (pdb code 1bhl). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Cacodylated Catalytic Domain of Hiv-1 Integrase, PDB code: 1bhl:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Cacodylated Catalytic Domain of Hiv-1 Integrase


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Cacodylated Catalytic Domain of Hiv-1 Integrase within 5.0Å range: probe atom residue distance (Å) B Occ A:As65 b:33.8 occ:1.00 AS A:CAS65 0.0 33.8 1.0 CE1 A:CAS65 1.9 30.9 1.0 CE2 A:CAS65 1.9 29.2 1.0 SG A:CAS65 2.2 29.1 1.0 CB A:CAS65 3.0 29.3 1.0 OD1 A:ASN120 3.5 30.1 1.0 ND2 A:ASN120 3.5 25.7 1.0 N A:CAS65 3.6 27.9 1.0 CG A:ASN120 3.6 30.4 1.0 CG A:GLU92 3.8 42.3 1.0 CA A:CAS65 3.9 30.2 1.0 OE2 A:GLU92 4.0 49.4 1.0 O A:HOH221 4.1 32.0 1.0 C A:ASP64 4.2 27.0 1.0 CD1 A:LEU74 4.2 36.9 1.0 CD A:GLU92 4.2 44.3 1.0 OG1 A:THR97 4.5 27.0 1.0 O A:HOH238 4.6 43.3 1.0 CA A:ASP64 4.7 26.3 1.0 CB A:ASN120 4.7 28.5 1.0 O A:HOH230 4.8 44.8 1.0 O A:ASP64 4.8 26.5 1.0 O A:HOH208 4.9 25.0 1.0

Arsenic binding site 2 out of 2 in the Cacodylated Catalytic Domain of Hiv-1 Integrase


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Cacodylated Catalytic Domain of Hiv-1 Integrase within 5.0Å range: probe atom residue distance (Å) B Occ A:As130 b:37.3 occ:1.00 AS A:CAS130 0.0 37.3 1.0 CE1 A:CAS130 1.7 29.2 1.0 CE2 A:CAS130 1.8 27.2 1.0 SG A:CAS130 2.3 28.1 1.0 CB A:CAS130 3.2 23.8 1.0 CG2 A:ILE135 4.2 27.7 1.0 O A:ILE135 4.2 29.8 1.0 N A:GLN137 4.3 38.3 1.0 C A:LYS136 4.4 35.4 1.0 O A:LYS136 4.5 31.4 1.0 CA A:GLN137 4.5 42.5 1.0 CA A:CAS130 4.6 22.6 1.0 C A:ILE135 4.6 31.7 1.0 CB A:GLN137 4.7 44.9 1.0 CB A:ILE135 4.7 28.1 1.0 CD2 A:PHE121 4.8 22.2 1.0 NE2 A:GLN137 4.9 47.7 1.0 CA A:LYS136 4.9 35.5 1.0 CG1 A:VAL126 4.9 21.4 1.0 CG A:GLN137 5.0 46.7 1.0 N A:LYS136 5.0 33.1 1.0

S.Maignan, J.P.Guilloteau, Q.Zhou-Liu, C.Clement-Mella, V.Mikol. Crystal Structures of the Catalytic Domain of Hiv-1 Integrase Free and Complexed with Its Metal Cofactor: High Level of Similarity of the Active Site with Other Viral Integrases. J.Mol.Biol. V. 282 359 1998.
ISSN: ISSN 0022-2836
PubMed: 9735293
DOI: 10.1006/JMBI.1998.2002