Calcium in PDB 7jnb: 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: 7jnb 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)	46.51 / 2.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	89.61, 89.61, 185.87, 90, 90, 90
R / Rfree (%)	20.9 / 23.5

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 7jnb). 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: 7jnb:
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:Ca501 b:43.9 occ:1.00 OD1 A:ASP321 2.2 40.0 1.0 O A:LYS318 2.3 45.6 1.0 O A:ASN426 2.3 35.8 1.0 OE2 A:GLU427 2.4 38.5 1.0 O A:THR326 2.5 51.0 1.0 O A:ASP323 2.5 38.5 1.0 OG1 A:THR326 2.6 46.5 1.0 CG A:ASP321 3.2 42.7 1.0 C A:THR326 3.3 52.7 1.0 C A:LYS318 3.4 47.5 1.0 C A:ASN426 3.5 37.9 1.0 CD A:GLU427 3.6 38.6 1.0 C A:ASP323 3.6 36.1 1.0 OD2 A:ASP321 3.7 45.7 1.0 CB A:THR326 3.8 48.8 1.0 N A:ASP323 3.9 37.4 1.0 CA A:THR326 3.9 51.9 1.0 CG A:GLU427 4.0 36.3 1.0 CA A:ASP323 4.1 36.6 1.0 N A:THR326 4.1 52.7 1.0 N A:ASP321 4.2 38.8 1.0 CA A:LYS318 4.3 51.3 1.0 CB A:ASP323 4.3 36.9 1.0 N A:TYR327 4.3 52.5 1.0 CA A:ASN426 4.3 38.5 1.0 N A:ALA319 4.4 42.7 1.0 CA A:ALA319 4.5 38.8 1.0 CB A:ASP321 4.5 40.1 1.0 C A:ALA319 4.5 35.7 1.0 CB A:LYS318 4.5 53.6 1.0 N A:GLU427 4.6 35.7 1.0 OE1 A:GLU427 4.6 38.4 1.0 N A:ILE320 4.6 33.3 1.0 N A:ASN322 4.7 38.9 1.0 N A:VAL324 4.7 36.7 1.0 CA A:TYR327 4.7 55.9 1.0 CA A:ASP321 4.7 40.3 1.0 CA A:GLU427 4.8 35.9 1.0 O A:ALA319 4.9 34.9 1.0 C A:ASP321 4.9 40.7 1.0 CG2 A:THR326 4.9 48.4 1.0 CB A:ASN426 4.9 38.8 1.0 CA A:VAL324 5.0 41.6 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:Ca502 b:30.8 occ:1.00 O A:LYS93 2.2 28.2 1.0 O A:ASN98 2.2 34.7 1.0 O A:THR101 2.3 31.2 1.0 OE2 A:GLU205 2.3 30.6 1.0 O A:ALA204 2.4 25.4 1.0 OG1 A:THR101 2.6 30.3 1.0 OD1 A:ASP96 2.6 32.6 1.0 C A:THR101 3.2 29.9 1.0 C A:ASN98 3.4 35.3 1.0 C A:LYS93 3.4 29.1 1.0 CD A:GLU205 3.4 30.6 1.0 CG A:ASP96 3.5 33.0 1.0 C A:ALA204 3.6 24.9 1.0 CB A:THR101 3.7 30.9 1.0 CA A:THR101 3.8 31.2 1.0 OD2 A:ASP96 3.8 33.8 1.0 CG A:GLU205 3.9 30.3 1.0 N A:ASN98 4.0 35.6 1.0 N A:THR101 4.0 32.6 1.0 CA A:ASN98 4.1 34.9 1.0 N A:HIS102 4.2 26.7 1.0 CA A:LYS93 4.3 28.6 1.0 CA A:ALA204 4.3 23.8 1.0 CB A:ASN98 4.3 35.7 1.0 N A:ALA94 4.4 27.7 1.0 N A:ASP96 4.4 30.4 1.0 N A:LEU99 4.4 31.8 1.0 CA A:ALA94 4.4 29.7 1.0 C A:ALA94 4.5 31.1 1.0 OE1 A:GLU205 4.5 31.2 1.0 CA A:HIS102 4.6 26.4 1.0 N A:GLU205 4.6 25.2 1.0 CA A:LEU99 4.7 34.0 1.0 CB A:LYS93 4.7 29.0 1.0 CA A:GLU205 4.7 26.2 1.0 CB A:ASP96 4.8 34.1 1.0 N A:ILE95 4.8 29.7 1.0 O A:ALA94 4.8 34.3 1.0 N A:GLY97 4.8 34.9 1.0 C A:LEU99 4.9 34.3 1.0 CG2 A:THR101 4.9 31.7 1.0 CB A:GLU205 4.9 27.8 1.0 CA A:ASP96 4.9 33.8 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.