Chlorine in PDB 1sp5: Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis

All present enzymatic activity of Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis:
3.4.23.16;

The structure of Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis, PDB code: 1sp5 was solved by E.Vondrackova, J.Hasek, M.Jaskolski, P.Rezacova, J.Dohnalek, T.Skalova, H.Petrokova, J.Duskova, J.Brynda, J.Sedlacek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.10 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.765, 86.284, 45.834, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 21.1

The binding sites of Chlorine atom in the Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis (pdb code 1sp5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis, PDB code: 1sp5:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis


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 Hiv-1 Protease Complexed with A Product of Autoproteolysis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:16.6 occ:1.00 NE1 A:TRP6 3.3 9.1 1.0 O B:HOH611 3.3 10.9 1.0 CZ2 A:TRP6 3.8 8.7 1.0 CE2 A:TRP6 3.9 10.9 1.0 CG2 A:THR4 4.2 12.9 1.0 O A:HOH649 4.4 38.3 1.0 CD1 A:TRP6 4.5 9.4 1.0 CB A:THR4 4.9 11.1 1.0 O B:HOH609 5.0 8.9 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl602 b:15.7 occ:1.00 O A:HOH609 3.0 13.8 1.0 N A:THR74 3.2 9.7 1.0 ND2 A:ASN88 3.2 7.4 1.0 CA A:GLY73 3.8 8.4 1.0 CB A:ASN88 3.8 6.5 1.0 OG1 A:THR74 3.9 12.1 1.0 CB A:THR74 3.9 10.2 1.0 C A:GLY73 4.0 11.0 1.0 CG A:ASN88 4.0 7.1 1.0 CA A:THR74 4.2 10.2 1.0 NE2 A:GLN92 4.2 8.9 1.0 O A:HOH607 4.3 12.0 1.0 O A:ASN88 4.5 8.1 1.0 CD2 A:LEU89 4.7 8.9 1.0 CA A:ASN88 4.8 7.3 1.0 O A:THR74 4.8 9.0 1.0 C A:ASN88 4.8 9.3 1.0 C A:THR74 5.0 9.6 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Hiv-1 Protease Complexed with A Product of Autoproteolysis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl603 b:18.3 occ:1.00 ND2 B:ASN88 3.2 8.9 1.0 N B:THR74 3.3 11.9 1.0 OG1 B:THR74 3.7 14.4 1.0 CB B:ASN88 3.8 6.8 1.0 CB B:THR74 3.8 12.8 1.0 CA B:GLY73 3.9 9.9 1.0 CG B:ASN88 4.0 9.1 1.0 C B:GLY73 4.1 12.3 1.0 CA B:THR74 4.2 11.1 1.0 O B:HOH613 4.2 16.5 1.0 O B:ASN88 4.8 10.1 1.0 O B:THR74 4.9 10.7 1.0 CA B:ASN88 4.9 7.2 1.0

E.Vondrackova, J.Hasek, M.Jaskolski, P.Rezacova, J.Dohnalek, T.Skalova, H.Petrokova, J.Duskova, J.Brynda, J.Sedlacek. Product of Enzymatic Self-Cleavage Bound in the Active Site of Hiv Protease To Be Published.