Chlorine in PDB 6pzp: Crystal Structure of Caspase-1 in Complex with Vx-765

All present enzymatic activity of Crystal Structure of Caspase-1 in Complex with Vx-765:
3.4.22.36;

The structure of Crystal Structure of Caspase-1 in Complex with Vx-765, PDB code: 6pzp was solved by J.Yang, Z.Liu, T.S.Xiao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.89 / 1.94
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	63.605, 63.605, 162.107, 90.00, 90.00, 90.00
R / Rfree (%)	16.7 / 20.8

The binding sites of Chlorine atom in the Crystal Structure of Caspase-1 in Complex with Vx-765 (pdb code 6pzp). 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 Caspase-1 in Complex with Vx-765, PDB code: 6pzp:

Chlorine binding site 1 out of 1 in the Crystal Structure of Caspase-1 in Complex with Vx-765


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 Caspase-1 in Complex with Vx-765 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:64.8 occ:1.00 CL33 A:P7S301 0.0 64.8 1.0 C28 A:P7S301 1.8 59.8 1.0 C27 A:P7S301 2.7 58.5 1.0 C29 A:P7S301 2.8 61.8 1.0 N32 A:P7S301 3.0 64.9 1.0 CG2 B:VAL348 3.3 46.8 1.0 NE B:ARG383 3.6 61.7 1.0 CB B:HIS342 3.7 49.0 1.0 N B:HIS342 3.8 45.4 1.0 C26 A:P7S301 4.0 57.1 1.0 O A:HOH492 4.0 72.4 1.0 CA B:HIS342 4.0 48.6 1.0 C30 A:P7S301 4.0 63.7 1.0 CD B:ARG383 4.1 60.0 1.0 O B:HOH555 4.2 56.4 1.0 C B:ARG341 4.2 47.0 1.0 O B:HOH531 4.2 55.4 1.0 CZ B:ARG383 4.2 71.3 1.0 NH2 B:ARG383 4.4 67.7 1.0 CB B:TRP340 4.4 39.1 1.0 O B:ARG341 4.5 50.2 1.0 C31 A:P7S301 4.5 62.0 1.0 CG B:HIS342 4.5 64.0 1.0 CD2 B:HIS342 4.6 68.7 1.0 O B:HOH544 4.6 54.0 1.0 N B:ARG341 4.7 40.4 1.0 CB B:VAL348 4.8 37.6 1.0 CA B:ARG341 4.8 41.1 1.0 C B:TRP340 4.9 36.9 1.0

J.Yang, Z.Liu, T.S.Xiao. Crystal Structure of Caspase-1 in Complex with Vx-765 To Be Published.