Chlorine in PDB 2r9f: Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide

All present enzymatic activity of Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide:
3.4.22.52;

The structure of Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide, PDB code: 2r9f was solved by J.Qian, R.L.Campbell, P.L.Davies, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.29 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.569, 70.568, 110.406, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 22.2

The structure of Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Chlorine atom in the Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide (pdb code 2r9f). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide, PDB code: 2r9f:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl663 b:15.9 occ:1.00 O A:HOH425 3.0 15.2 1.0 N A:PHE141 3.2 11.7 1.0 N A:PHE97 3.2 9.1 1.0 NE2 A:GLN142 3.3 23.7 1.0 OE1 A:GLN142 3.4 27.8 1.0 NE2 A:GLN96 3.4 18.1 1.0 CB A:SER140 3.4 14.6 1.0 CA A:SER140 3.5 13.1 1.0 CA A:GLN96 3.7 8.8 1.0 CD A:GLN142 3.7 24.1 1.0 C A:SER140 3.9 12.8 1.0 CD1 A:PHE141 3.9 8.8 1.0 C A:GLN96 4.0 8.2 1.0 CD A:GLN96 4.0 17.8 1.0 CB A:PHE97 4.1 8.4 1.0 O A:PRO95 4.2 9.7 1.0 CA A:PHE97 4.3 7.9 1.0 CA A:PHE141 4.3 12.7 1.0 CB A:PHE141 4.3 11.8 1.0 CB A:GLN96 4.4 9.1 1.0 OE1 A:GLN96 4.4 22.4 1.0 OG A:SER140 4.5 15.4 1.0 O A:GLN139 4.5 13.5 1.0 CG A:PHE141 4.6 10.4 1.0 N A:GLN142 4.7 15.7 1.0 N A:GLN96 4.8 8.7 1.0 CG A:GLN96 4.8 12.3 1.0 N A:SER140 4.8 13.1 1.0 C A:PRO95 4.9 9.2 1.0 CE1 A:PHE141 4.9 8.8 1.0 C A:PHE141 4.9 14.2 1.0

Chlorine binding site 2 out of 3 in the Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl664 b:16.4 occ:1.00 O A:HOH414 3.0 12.1 1.0 OE1 A:GLN40 3.2 8.2 1.0 O A:HOH444 3.3 18.7 1.0 O A:HOH530 3.4 21.9 1.0 CG A:GLN40 3.9 6.1 1.0 CD A:GLN40 4.0 6.5 1.0 CD2 A:LEU45 4.1 9.3 1.0 CD1 A:LEU45 4.2 9.7 1.0 CE1 A:PHE56 4.3 6.7 1.0 CZ A:PHE56 4.4 6.8 1.0 CB A:GLN40 4.8 6.0 1.0 CG A:LEU45 4.8 8.5 1.0 OD2 A:ASP59 4.9 16.4 1.0

Chlorine binding site 3 out of 3 in the Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Calpain 1 Proteolytic Core Inactivated By Zlak-3002, An Alpha- Ketoamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl665 b:14.4 occ:1.00 O A:HOH507 2.9 22.5 1.0 OG A:SER65 3.1 11.3 1.0 CB A:SER65 3.5 9.4 1.0 CB A:PRO75 4.2 20.4 1.0 O A:PRO75 4.3 22.5 1.0 CA A:PRO75 4.3 20.5 1.0 N A:SER65 4.7 7.6 1.0 CA A:SER65 4.7 8.7 1.0 C A:PRO75 4.8 21.6 1.0 CG2 A:THR80 5.0 20.3 1.0

J.Qian, D.Cuerrier, P.L.Davies, Z.Li, J.C.Powers, R.L.Campbell. Cocrystal Structures of Primed Side-Extending Alpha-Ketoamide Inhibitors Reveal Novel Calpain-Inhibitor Aromatic Interactions. J.Med.Chem. V. 51 5264 2008.
ISSN: ISSN 0022-2623
PubMed: 18702462
DOI: 10.1021/JM800045T