Calcium in PDB 7jnf: The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb in Complex with Galnac

The structure of The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb in Complex with Galnac, PDB code: 7jnf was solved by B.Pluvinage, A.B.Boraston, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.57 / 2.10
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	89.74, 89.74, 187.49, 90, 90, 90
R / Rfree (%)	23.1 / 25.6

The binding sites of Calcium atom in the The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb in Complex with Galnac (pdb code 7jnf). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb in Complex with Galnac, PDB code: 7jnf:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb in Complex with Galnac


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb in Complex with Galnac within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca502 b:33.7 occ:1.00 O A:LYS93 2.3 28.0 1.0 O A:ASN98 2.3 35.9 1.0 O A:THR101 2.4 32.3 1.0 OD1 A:ASP96 2.4 32.2 1.0 O A:ALA204 2.4 26.9 1.0 OE2 A:GLU205 2.5 31.3 1.0 OG1 A:THR101 2.7 32.9 1.0 C A:THR101 3.3 32.0 1.0 CG A:ASP96 3.4 32.1 1.0 C A:ASN98 3.4 36.2 1.0 C A:LYS93 3.5 28.1 1.0 CD A:GLU205 3.6 31.5 1.0 C A:ALA204 3.6 26.4 1.0 OD2 A:ASP96 3.8 32.0 1.0 CB A:THR101 3.9 33.2 1.0 N A:ASN98 3.9 35.5 1.0 CA A:THR101 4.0 33.1 1.0 CG A:GLU205 4.0 30.5 1.0 CA A:ASN98 4.1 35.8 1.0 N A:THR101 4.1 34.8 1.0 N A:HIS102 4.3 29.4 1.0 CA A:LYS93 4.3 28.0 1.0 CB A:ASN98 4.4 35.6 1.0 CA A:ALA204 4.4 25.7 1.0 N A:ALA94 4.4 27.9 1.0 N A:ASP96 4.4 31.1 1.0 N A:LEU99 4.4 36.6 1.0 CA A:ALA94 4.5 28.4 1.0 C A:ALA94 4.5 28.8 1.0 N A:GLU205 4.6 27.1 1.0 CA A:HIS102 4.6 28.0 1.0 CB A:ASP96 4.6 32.2 1.0 OE1 A:GLU205 4.6 32.7 1.0 CA A:LEU99 4.7 37.0 1.0 CB A:LYS93 4.7 28.3 1.0 N A:GLY97 4.7 34.6 1.0 CA A:GLU205 4.8 27.9 1.0 N A:ILE95 4.8 28.2 1.0 C A:LEU99 4.8 37.6 1.0 O A:ALA94 4.9 28.6 1.0 CA A:ASP96 4.9 32.4 1.0 CB A:GLU205 5.0 28.7 1.0

Calcium binding site 2 out of 2 in the The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb in Complex with Galnac


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Structure of CBM32-1 and CBM32-2 Domains From Clostridium Perfringens Zmpb in Complex with Galnac within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca503 b:44.1 occ:1.00 O A:ASN426 2.2 39.7 1.0 OD1 A:ASP321 2.3 41.4 1.0 O A:LYS318 2.3 43.9 1.0 O A:ASP323 2.4 40.5 1.0 O A:THR326 2.5 54.1 1.0 OE2 A:GLU427 2.5 40.9 1.0 OG1 A:THR326 2.6 49.4 1.0 C A:THR326 3.4 54.2 1.0 CG A:ASP321 3.4 43.0 1.0 C A:LYS318 3.4 44.9 1.0 C A:ASN426 3.4 40.3 1.0 C A:ASP323 3.5 40.5 1.0 CD A:GLU427 3.5 40.3 1.0 CB A:THR326 3.8 51.4 1.0 N A:ASP323 3.9 40.3 1.0 OD2 A:ASP321 3.9 44.7 1.0 CG A:GLU427 3.9 39.6 1.0 CA A:THR326 4.0 52.5 1.0 CA A:ASP323 4.0 39.9 1.0 N A:THR326 4.1 52.4 1.0 CB A:ASP323 4.2 39.3 1.0 CA A:LYS318 4.2 46.3 1.0 CA A:ASN426 4.3 42.0 1.0 N A:ALA319 4.3 43.2 1.0 N A:ASP321 4.3 40.9 1.0 N A:TYR327 4.4 55.3 1.0 CA A:ALA319 4.4 41.8 1.0 N A:GLU427 4.4 39.4 1.0 C A:ALA319 4.5 40.4 1.0 CB A:LYS318 4.5 47.1 1.0 N A:VAL324 4.6 41.9 1.0 CA A:GLU427 4.6 38.8 1.0 OE1 A:GLU427 4.6 40.9 1.0 CB A:ASP321 4.6 42.4 1.0 N A:ILE320 4.7 39.4 1.0 CA A:TYR327 4.7 56.8 1.0 N A:ASN322 4.8 40.6 1.0 CA A:ASP321 4.8 41.8 1.0 O A:ALA319 4.8 40.1 1.0 CB A:GLU427 4.9 39.0 1.0 CA A:VAL324 4.9 44.2 1.0 CG2 A:THR326 4.9 50.7 1.0 CB A:ASN426 4.9 42.4 1.0 C A:ASP321 5.0 41.4 1.0

B.Pluvinage, E.Ficko-Blean, I.Noach, C.Stuart, N.Thompson, H.Mcclure, N.Buenbrazo, W.Wakarchuck, A.B.Boraston. Molecular Insights Into Architecturally Complex Glycopeptidases To Be Published.