Magnesium in PDB 2b0q: Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex

All present enzymatic activity of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex:
2.7.1.95;

The structure of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex, PDB code: 2b0q was solved by D.H.Fong, A.M.Berghuis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.36 / 2.70
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	46.357, 46.357, 301.613, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 31.2

The binding sites of Magnesium atom in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex (pdb code 2b0q). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex, PDB code: 2b0q:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:15.6 occ:1.00 O2A A:ADP300 2.2 29.3 1.0 O A:HOH519 2.3 38.6 1.0 OD1 A:ASN195 2.3 30.0 1.0 O3B A:ADP300 2.5 30.4 1.0 OG A:SER194 2.8 38.4 1.0 OD2 A:ASP208 3.2 29.1 1.0 O3' A:ADP300 3.3 32.0 1.0 CG A:ASN195 3.4 32.6 1.0 PA A:ADP300 3.5 27.4 1.0 O A:SER194 3.6 32.9 1.0 O A:GLU24 3.8 70.9 1.0 CB A:SER194 3.9 37.2 1.0 PB A:ADP300 3.9 31.3 1.0 C3' A:ADP300 3.9 31.4 1.0 O3A A:ADP300 3.9 30.9 1.0 C A:SER194 4.0 34.1 1.0 C5' A:ADP300 4.0 28.8 1.0 ND2 A:ASN195 4.0 34.6 1.0 O5' A:ADP300 4.1 27.0 1.0 CG A:ASP208 4.3 31.9 1.0 C4' A:ADP300 4.4 31.3 1.0 N A:ASN195 4.5 32.8 1.0 CG A:GLU24 4.5 71.7 1.0 CA A:SER194 4.6 35.4 1.0 CB A:ASN195 4.6 31.5 1.0 O1B A:ADP300 4.6 31.7 1.0 CA A:ASN195 4.7 32.6 1.0 O1A A:ADP300 4.7 27.1 1.0 O A:HOH520 4.7 9.2 1.0 CB A:ASP208 4.8 31.5 1.0 C A:GLU24 4.8 69.9 1.0 O2B A:ADP300 4.8 31.9 1.0 OE2 A:GLU24 4.8 73.8 1.0 O3 A:NMY305 4.9 53.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Neomycin B Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:25.4 occ:1.00 O A:HOH520 2.1 9.2 1.0 OD1 A:ASP208 2.2 32.2 1.0 O1B A:ADP300 2.3 31.7 1.0 OD2 A:ASP208 2.8 29.1 1.0 CG A:ASP208 2.8 31.9 1.0 OD2 A:ASP190 3.4 38.0 1.0 PB A:ADP300 3.5 31.3 1.0 O3B A:ADP300 3.8 30.4 1.0 O3 A:NMY305 4.0 53.9 1.0 O4 A:NMY305 4.0 48.3 1.0 CB A:SER27 4.1 42.8 1.0 O A:HOH519 4.2 38.6 1.0 CB A:ASP208 4.3 31.5 1.0 O2B A:ADP300 4.3 31.9 1.0 OG A:SER27 4.5 40.8 1.0 NZ A:LYS44 4.5 30.8 1.0 CG A:ASP190 4.6 37.8 1.0 O3A A:ADP300 4.7 30.9 1.0 C3 A:NMY305 4.9 51.5 1.0 C4 A:NMY305 4.9 51.2 1.0 O2A A:ADP300 4.9 29.3 1.0 CA A:ASP208 5.0 32.1 1.0

D.H.Fong, A.M.Berghuis. Substrate Promiscuity of An Aminoglycoside Antibiotic Resistance Enzyme Via Target Mimicry. Embo J. V. 21 2323 2002.
ISSN: ISSN 0261-4189
PubMed: 12006485
DOI: 10.1093/EMBOJ/21.10.2323