Chlorine in PDB 1g0z: Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution

All present enzymatic activity of Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution:
3.1.1.4;

The structure of Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution, PDB code: 1g0z was solved by T.P.Singh, S.Gourinath, S.Sharma, G.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.26 / 2.18
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	80.360, 80.360, 99.440, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 25.7

The binding sites of Chlorine atom in the Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution (pdb code 1g0z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution, PDB code: 1g0z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl121 b:23.5 occ:1.00 O A:HOH167 2.9 22.1 1.0 N A:THR82 3.3 20.7 1.0 N A:SER83 3.4 22.7 1.0 OG A:SER83 3.8 28.6 1.0 CB A:THR82 3.8 21.4 1.0 CB A:SER83 3.9 25.2 1.0 CA A:THR82 4.0 21.2 1.0 O A:HOH197 4.1 45.8 1.0 C A:THR82 4.2 22.0 1.0 CA A:ASP81 4.2 19.2 1.0 C A:ASP81 4.2 19.4 1.0 CA A:SER83 4.3 24.3 1.0 O A:ASN80 4.4 19.8 1.0 OG1 A:THR82 4.4 23.1 1.0 OD1 A:ASP81 4.8 19.8 1.0 N A:ASP84 4.9 22.6 1.0

Chlorine binding site 2 out of 2 in the Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl121 b:21.9 occ:1.00 O B:HOH186 2.9 29.0 1.0 N B:THR82 3.3 21.1 1.0 N B:SER83 3.5 23.0 1.0 CB B:THR82 3.8 21.5 1.0 OG B:SER83 3.8 28.3 1.0 O B:HOH206 3.9 34.7 1.0 CA B:THR82 4.0 21.8 1.0 CB B:SER83 4.1 24.7 1.0 O B:ASN80 4.2 20.4 1.0 CA B:ASP81 4.2 19.4 1.0 C B:ASP81 4.2 19.5 1.0 C B:THR82 4.3 22.3 1.0 OG1 B:THR82 4.3 22.9 1.0 CA B:SER83 4.4 23.7 1.0 OD1 B:ASP81 4.9 20.0 1.0

S.Gourinath, G.Singh, S.Sharma, S.Bhanumathi, C.Betzel, M.Paramsivam, A.Srinivasan, T.P.Singh. Specific Mutations in Krait PLA2 Lead to Dimerization of Protein Molecules: Crystal Structure of Krait PLA2 at 2.1 Resolution. To Be Published.