Magnesium in PDB 1j7u: Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Complex

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

The structure of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Complex, PDB code: 1j7u was solved by D.L.Burk, W.C.Hon, A.K.-W.Leung, A.M.Berghuis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.80 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.168, 91.321, 132.653, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 27.7

The binding sites of Magnesium atom in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Complex (pdb code 1j7u). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Complex, PDB code: 1j7u:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp 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 Amppnp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:29.4 occ:1.00 O1G A:ANP303 2.0 46.4 1.0 O A:HOH349 2.0 60.5 1.0 OD1 A:ASN195 2.1 25.2 1.0 O2A A:ANP303 2.1 25.2 1.0 OD2 A:ASP208 2.3 16.8 1.0 N3B A:ANP303 2.7 37.7 1.0 O A:HOH390 2.9 42.0 1.0 PG A:ANP303 3.0 45.2 1.0 CG A:ASN195 3.0 21.7 1.0 CG A:ASP208 3.3 17.8 1.0 ND2 A:ASN195 3.4 23.8 1.0 PA A:ANP303 3.5 25.7 1.0 CB A:ASP208 3.7 15.5 1.0 MG A:MG302 3.9 28.2 1.0 O3G A:ANP303 3.9 42.9 1.0 O A:HOH393 3.9 42.2 1.0 PB A:ANP303 3.9 30.6 1.0 O2G A:ANP303 4.1 44.0 1.0 O3A A:ANP303 4.2 30.5 1.0 O2B A:ANP303 4.2 34.2 1.0 O A:SER194 4.3 28.8 1.0 O3' A:ANP303 4.4 23.9 1.0 OD1 A:ASP208 4.4 16.9 1.0 CB A:ASN195 4.4 22.5 1.0 O1A A:ANP303 4.4 24.9 1.0 O5' A:ANP303 4.5 24.8 1.0 OD2 A:ASP190 4.5 20.2 1.0 C A:SER194 4.6 27.7 1.0 CB A:SER194 4.7 30.3 1.0 C5' A:ANP303 4.7 23.4 1.0 O A:HOH348 4.7 18.7 1.0 C3' A:ANP303 4.8 22.3 1.0 CA A:ASN195 4.9 24.2 1.0 N A:ASN195 4.9 25.6 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp 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 Amppnp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:28.2 occ:1.00 O3G A:ANP303 2.0 42.9 1.0 O2B A:ANP303 2.0 34.2 1.0 O A:HOH347 2.1 28.3 1.0 O A:HOH348 2.1 18.7 1.0 OD2 A:ASP208 2.2 16.8 1.0 OD1 A:ASP208 2.4 16.9 1.0 CG A:ASP208 2.6 17.8 1.0 PG A:ANP303 2.9 45.2 1.0 PB A:ANP303 3.0 30.6 1.0 N3B A:ANP303 3.0 37.7 1.0 O1G A:ANP303 3.4 46.4 1.0 MG A:MG301 3.9 29.4 1.0 O1B A:ANP303 4.0 34.2 1.0 OD2 A:ASP190 4.0 20.2 1.0 CB A:ASP208 4.1 15.5 1.0 O2G A:ANP303 4.2 44.0 1.0 O3A A:ANP303 4.2 30.5 1.0 O A:HOH382 4.3 19.9 1.0 O2A A:ANP303 4.3 25.2 1.0 O A:HOH310 4.3 16.9 1.0 NZ A:LYS44 4.4 18.3 1.0 O A:HOH373 4.5 18.7 1.0 CB A:SER27 4.6 49.4 1.0 PA A:ANP303 4.7 25.7 1.0 OG A:SER27 4.7 46.9 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:29.6 occ:1.00 O2A B:ANP304 1.9 29.8 1.0 O1G B:ANP304 2.0 44.0 1.0 OD2 B:ASP208 2.2 16.5 1.0 O B:HOH390 2.2 40.8 1.0 N3B B:ANP304 2.4 37.7 1.0 OD1 B:ASN195 2.4 26.0 1.0 O B:HOH391 2.8 70.4 1.0 PG B:ANP304 2.8 45.9 1.0 CG B:ASP208 3.1 18.1 1.0 PA B:ANP304 3.2 27.9 1.0 CG B:ASN195 3.4 24.9 1.0 PB B:ANP304 3.5 33.4 1.0 CB B:ASP208 3.6 16.4 1.0 O3G B:ANP304 3.6 45.4 1.0 O B:HOH399 3.7 35.4 1.0 ND2 B:ASN195 3.7 23.1 1.0 MG B:MG302 3.7 26.5 1.0 O3A B:ANP304 3.8 31.0 1.0 O2B B:ANP304 3.8 34.1 1.0 O2G B:ANP304 3.9 43.9 1.0 O B:HOH341 4.0 45.3 1.0 O1A B:ANP304 4.1 27.4 1.0 OD1 B:ASP208 4.1 14.6 1.0 OG B:SER194 4.2 26.2 1.0 O5' B:ANP304 4.3 28.2 1.0 O B:SER194 4.4 22.1 1.0 OD2 B:ASP190 4.4 21.5 1.0 O B:HOH353 4.4 21.7 1.0 O3' B:ANP304 4.5 23.2 1.0 C5' B:ANP304 4.5 25.0 1.0 O1B B:ANP304 4.7 34.6 1.0 CB B:ASN195 4.7 24.8 1.0 C3' B:ANP304 4.8 22.2 1.0 C B:SER194 4.9 25.8 1.0 CA B:ASP208 4.9 14.6 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Amppnp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:26.5 occ:1.00 O B:HOH353 1.9 21.7 1.0 O3G B:ANP304 2.0 45.4 1.0 O B:HOH354 2.0 26.6 1.0 OD2 B:ASP208 2.1 16.5 1.0 O2B B:ANP304 2.2 34.1 1.0 OD1 B:ASP208 2.4 14.6 1.0 CG B:ASP208 2.6 18.1 1.0 PG B:ANP304 3.0 45.9 1.0 PB B:ANP304 3.2 33.4 1.0 N3B B:ANP304 3.2 37.7 1.0 O1G B:ANP304 3.5 44.0 1.0 MG B:MG301 3.7 29.6 1.0 OD2 B:ASP190 4.0 21.5 1.0 CB B:ASP208 4.1 16.4 1.0 O B:HOH310 4.1 16.7 1.0 O1B B:ANP304 4.1 34.6 1.0 O B:HOH321 4.2 12.2 1.0 CB B:SER27 4.3 42.8 1.0 O B:HOH333 4.3 18.1 1.0 O2G B:ANP304 4.4 43.9 1.0 OG B:SER27 4.4 41.6 1.0 O3A B:ANP304 4.5 31.0 1.0 O B:HOH315 4.5 14.4 1.0 O2A B:ANP304 4.5 29.8 1.0 NZ B:LYS44 4.5 10.9 1.0 PA B:ANP304 4.9 27.9 1.0 CG B:ASP190 5.0 22.9 1.0 CA B:ASP208 5.0 14.6 1.0

D.L.Burk, W.C.Hon, A.K.Leung, A.M.Berghuis. Structural Analyses of Nucleotide Binding to An Aminoglycoside Phosphotransferase. Biochemistry V. 40 8756 2001.
ISSN: ISSN 0006-2960
PubMed: 11467935
DOI: 10.1021/BI010504P