Calcium in PDB 2bue: Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A.

All present enzymatic activity of Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A.:
2.3.1.82;

The structure of Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A., PDB code: 2bue was solved by M.W.Vetting, C.H.Park, S.S.Hedge, D.C.Hooper, J.S.Blanchard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	149.07 / 1.70
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	57.475, 57.475, 148.305, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 21.1

The binding sites of Calcium atom in the Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A. (pdb code 2bue). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A., PDB code: 2bue:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1202 b:13.2 occ:1.00 OE2 A:GLU145 2.3 16.1 1.0 O A:HOH2177 2.4 22.2 1.0 O A:HOH2172 2.4 14.9 1.0 O A:HOH2182 2.5 35.1 1.0 CD A:GLU145 3.3 18.2 1.0 CG A:GLU145 3.9 14.1 1.0 OE1 A:GLU145 4.3 23.6 1.0 O A:HOH2179 4.4 21.9 1.0 OD1 A:ASP143 4.5 11.7 1.0 O A:HOH2094 4.6 31.2 1.0

Calcium binding site 2 out of 2 in the Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Aac(6')-Ib in Complex with Ribostamycin and Coenzyme A. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1203 b:18.6 occ:1.00 O A:HOH2236 2.3 21.6 1.0 O A:ARG194 2.4 18.9 1.0 O A:ALA199 2.4 31.8 1.0 O A:SER197 2.4 25.1 1.0 C A:ARG194 3.5 18.1 1.0 C A:SER197 3.6 25.8 1.0 C A:ALA199 3.7 32.3 1.0 CA A:ARG194 4.0 17.1 1.0 N A:ALA199 4.3 31.6 1.0 OG A:SER197 4.3 26.4 1.0 O A:HOH2237 4.3 45.5 1.0 C A:ASP198 4.4 30.9 1.0 OXT A:ALA199 4.4 32.5 1.0 N A:SER197 4.4 23.6 1.0 N A:ASP198 4.5 27.8 1.0 CA A:ASP198 4.5 30.4 1.0 CA A:SER197 4.5 24.9 1.0 CA A:ALA199 4.6 32.0 1.0 N A:THR195 4.6 17.9 1.0 CB A:ARG194 4.7 17.4 1.0 O A:ASP198 4.9 31.1 1.0 O A:GLU193 4.9 14.9 1.0 CA A:THR195 4.9 19.5 1.0

M.W.Vetting, C.H.Park, S.S.Hegde, G.A.Jacoby, D.C.Hooper, J.S.Blanchard. Mechanistic and Structural Analysis of Aminoglycoside N-Acetyltransferase Aac(6')-Ib and Its Bifunctional, Fluoroquinolone-Active Aac(6')-Ib-Cr Variant. Biochemistry V. 47 9825 2008.
ISSN: ISSN 0006-2960
PubMed: 18710261
DOI: 10.1021/BI800664X