Magnesium in PDB 1nd4: Crystal Structure of Aminoglycoside-3'-Phosphotransferase- Iia

All present enzymatic activity of Crystal Structure of Aminoglycoside-3'-Phosphotransferase- Iia:
2.7.1.95;

The structure of Crystal Structure of Aminoglycoside-3'-Phosphotransferase- Iia, PDB code: 1nd4 was solved by D.Nurizzo, S.C.Shewry, E.N.Baker, C.A.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	43.048, 101.893, 71.972, 90.00, 105.58, 90.00
R / Rfree (%)	20.6 / 23.8

The structure of Crystal Structure of Aminoglycoside-3'-Phosphotransferase- Iia also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Aminoglycoside-3'-Phosphotransferase- Iia (pdb code 1nd4). 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 Aminoglycoside-3'-Phosphotransferase- Iia, PDB code: 1nd4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Aminoglycoside-3'-Phosphotransferase- Iia


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 Aminoglycoside-3'-Phosphotransferase- Iia within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg400 b:46.5 occ:1.00 O A:HOH1615 2.1 30.7 1.0 OD2 A:ASP208 2.1 24.2 1.0 OD1 A:ASN195 2.2 25.2 1.0 O A:HOH1688 2.3 30.7 1.0 O A:HOH1637 2.4 44.7 1.0 CG A:ASN195 3.2 26.0 1.0 CG A:ASP208 3.2 24.4 1.0 ND2 A:ASN195 3.6 24.8 1.0 CB A:ASP208 3.8 23.9 1.0 O A:HOH1794 4.0 46.1 1.0 OD1 A:ASP208 4.3 25.8 1.0 NA A:NA1600 4.5 52.4 1.0 CB A:ASN195 4.6 24.1 1.0 O A:PRO194 4.6 26.2 1.0 O7 A:KAN1300 4.6 46.1 1.0 CD1 A:ILE207 4.7 26.9 1.0 C A:PRO194 4.8 26.4 1.0 CA A:ASN195 4.8 24.6 1.0 SG A:CYS192 4.9 31.1 0.5 N A:ASN195 4.9 24.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Aminoglycoside-3'-Phosphotransferase- Iia


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 Aminoglycoside-3'-Phosphotransferase- Iia within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg400 b:51.3 occ:1.00 OD2 B:ASP208 2.0 28.9 1.0 O B:HOH2744 2.1 34.4 1.0 OD1 B:ASN195 2.2 22.7 1.0 O B:HOH2734 2.4 36.6 1.0 O B:HOH2612 2.4 35.1 1.0 O B:HOH2697 2.8 46.9 1.0 CG B:ASP208 3.2 31.4 1.0 CG B:ASN195 3.2 22.9 1.0 ND2 B:ASN195 3.7 21.2 1.0 CB B:ASP208 3.8 26.6 1.0 OD1 B:ASP208 4.2 28.6 1.0 O B:PRO194 4.2 26.1 1.0 O B:HOH2714 4.2 54.9 1.0 CB B:ASN195 4.5 23.7 1.0 C B:PRO194 4.5 25.2 1.0 CD1 B:ILE207 4.6 27.9 1.0 CA B:ASN195 4.7 23.1 1.0 O7 B:KAN2300 4.7 50.7 1.0 N B:ASN195 4.8 22.8 1.0 SG B:CYS192 4.8 34.4 0.5 CB B:PRO194 4.8 23.5 1.0 NA B:NA2600 4.9 46.7 1.0 CG B:PRO194 5.0 25.6 1.0 CG1 B:ILE207 5.0 26.2 1.0

D.Nurizzo, S.C.Shewry, M.H.Perlin, S.A.Brown, J.N.Dholakia, R.L.Fuchs, T.Deva, E.N.Baker, C.A.Smith. The Crystal Structure of Aminoglycoside-3'-Phosphotransferase-Iia, An Enzyme Responsible For Antibiotic Resistance J.Mol.Biol. V. 327 491 2003.
ISSN: ISSN 0022-2836
PubMed: 12628253
DOI: 10.1016/S0022-2836(03)00121-9