Chlorine in PDB 6bgp: Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A

All present enzymatic activity of Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A:
3.4.22.54;

The structure of Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A, PDB code: 6bgp was solved by Q.Ye, 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)	17.94 / 2.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.100, 106.180, 225.620, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 25.8

The structure of Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A also contains other interesting chemical elements:

Calcium

(Ca)

8 atoms

The binding sites of Chlorine atom in the Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A (pdb code 6bgp). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A, PDB code: 6bgp:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A


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 Human Calpain-3 Protease Core Mutant-C129A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:47.6 occ:1.00 N A:PHE155 3.3 46.2 1.0 N A:PHE111 3.4 38.2 1.0 CD A:ARG110 3.4 52.9 1.0 OG A:SER154 3.4 51.1 1.0 CA A:ARG110 3.6 42.5 1.0 CA A:SER154 3.7 50.0 1.0 C A:ARG110 4.0 40.0 1.0 CB A:SER154 4.0 48.0 1.0 C A:SER154 4.0 48.9 1.0 CD2 A:PHE155 4.1 41.0 1.0 CB A:ARG110 4.1 47.8 1.0 CB A:PHE155 4.2 43.7 1.0 CG1 A:ILE156 4.2 62.8 1.0 CA A:PHE155 4.2 46.3 1.0 CB A:PHE111 4.3 37.6 1.0 N A:ILE156 4.3 52.8 1.0 O A:PRO109 4.4 43.4 1.0 CG A:ARG110 4.4 51.2 1.0 CA A:PHE111 4.4 37.9 1.0 NE A:ARG110 4.4 59.1 1.0 O A:GLN153 4.6 59.2 1.0 CG A:PHE155 4.6 42.0 1.0 CD1 A:ILE156 4.7 64.8 1.0 N A:ARG110 4.8 40.5 1.0 C A:PHE155 4.8 47.5 1.0 CG2 A:ILE156 4.8 57.5 1.0 NH1 A:ARG110 4.8 71.5 1.0 N A:SER154 4.9 52.7 1.0 C A:PRO109 5.0 43.0 1.0 CB A:ILE156 5.0 58.6 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A


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 Human Calpain-3 Protease Core Mutant-C129A within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl503 b:58.1 occ:1.00 N B:PHE111 3.2 38.9 1.0 N B:PHE155 3.4 62.7 1.0 CD B:ARG110 3.5 57.9 1.0 OG B:SER154 3.5 65.4 1.0 CA B:ARG110 3.6 47.4 1.0 CA B:SER154 3.7 59.8 1.0 C B:ARG110 3.9 43.6 1.0 CB B:PHE111 4.0 38.2 1.0 CB B:SER154 4.0 62.2 1.0 CB B:ARG110 4.1 48.4 1.0 C B:SER154 4.1 60.2 1.0 CD2 B:PHE155 4.1 71.3 1.0 CA B:PHE111 4.2 38.6 1.0 CB B:PHE155 4.3 72.1 1.0 CA B:PHE155 4.4 70.8 1.0 CG1 B:ILE156 4.4 78.7 1.0 CG B:ARG110 4.4 51.2 1.0 O B:GLN153 4.5 62.2 1.0 N B:ILE156 4.5 69.8 1.0 O B:PRO109 4.5 42.4 1.0 NE B:ARG110 4.6 65.5 1.0 CG B:PHE155 4.7 72.9 1.0 N B:ARG110 4.8 46.1 1.0 N B:ILE112 4.8 43.2 1.0 N B:SER154 4.8 60.0 1.0 NH1 B:ARG110 4.9 71.0 1.0 CD1 B:ILE156 4.9 82.0 1.0 C B:PHE155 5.0 71.2 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A


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 Human Calpain-3 Protease Core Mutant-C129A within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl503 b:46.5 occ:1.00 N C:PHE111 3.2 38.0 1.0 CD C:ARG110 3.3 62.5 1.0 N C:PHE155 3.4 46.4 1.0 CA C:ARG110 3.4 49.6 1.0 OG C:SER154 3.6 63.4 1.0 C C:ARG110 3.8 43.0 1.0 CA C:SER154 3.8 52.5 1.0 CB C:ARG110 3.9 53.3 1.0 CD2 C:PHE155 4.0 43.1 1.0 CB C:PHE111 4.1 41.5 1.0 C C:SER154 4.1 49.2 1.0 CB C:SER154 4.2 56.2 1.0 CB C:PHE155 4.2 46.7 1.0 CA C:PHE111 4.3 40.1 1.0 CG C:ARG110 4.3 56.6 1.0 O C:PRO109 4.3 44.5 1.0 CA C:PHE155 4.3 47.9 1.0 CG1 C:ILE156 4.4 65.4 1.0 NE C:ARG110 4.4 74.9 1.0 N C:ILE156 4.5 55.5 1.0 N C:ARG110 4.6 47.9 1.0 CG C:PHE155 4.6 45.9 1.0 O C:GLN153 4.7 52.4 1.0 NH1 C:ARG110 4.8 86.2 1.0 C C:PRO109 4.9 46.7 1.0 CD1 C:ILE156 4.9 69.0 1.0 C C:PHE155 4.9 54.3 1.0 CG2 C:ILE156 4.9 61.8 1.0 N C:ILE112 4.9 41.1 1.0 CE2 C:PHE155 5.0 42.5 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Human Calpain-3 Protease Core Mutant-C129A within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl503 b:53.0 occ:1.00 N D:PHE111 3.1 36.0 1.0 N D:PHE155 3.2 51.0 1.0 OG D:SER154 3.5 64.5 1.0 CA D:ARG110 3.6 45.1 1.0 CD D:ARG110 3.6 53.6 1.0 CA D:SER154 3.6 53.9 1.0 C D:ARG110 3.8 40.6 1.0 CD2 D:PHE155 3.9 48.9 1.0 C D:SER154 4.0 51.5 1.0 CB D:PHE111 4.0 31.6 1.0 CB D:SER154 4.0 57.4 1.0 CB D:ARG110 4.1 48.2 1.0 CB D:PHE155 4.1 49.2 1.0 CA D:PHE111 4.2 32.8 1.0 CA D:PHE155 4.2 51.9 1.0 O D:PRO109 4.4 44.9 1.0 N D:ILE156 4.5 54.5 1.0 CG1 D:ILE156 4.5 59.5 1.0 O D:GLN153 4.5 52.4 1.0 CG D:ARG110 4.5 51.5 1.0 CG D:PHE155 4.5 48.4 1.0 NE D:ARG110 4.7 57.3 1.0 N D:ARG110 4.7 46.4 1.0 N D:SER154 4.8 52.5 1.0 C D:PHE155 4.9 53.9 1.0 CE2 D:PHE155 4.9 44.9 1.0 N D:ILE112 4.9 34.1 1.0 C D:PRO109 5.0 48.5 1.0

Q.Ye, R.L.Campbell, P.L.Davies. Structures of Human Calpain-3 Protease Core with and Without Bound Inhibitor Reveal Mechanisms of Calpain Activation. J. Biol. Chem. V. 293 4056 2018.
ISSN: ESSN 1083-351X
PubMed: 29382717
DOI: 10.1074/JBC.RA117.001097