Magnesium in PDB 1j7l: Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Complex

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

The structure of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Complex, PDB code: 1j7l 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)	37.47 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.710, 91.245, 131.301, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 27.9

The binding sites of Magnesium atom in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Complex (pdb code 1j7l). 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 Adp Complex, PDB code: 1j7l:
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 Adp 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 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:17.9 occ:1.00 O3B A:ADP303 2.0 8.0 1.0 OD2 A:ASP208 2.0 11.3 1.0 O2A A:ADP303 2.1 11.2 1.0 O A:HOH438 2.1 14.9 1.0 OD1 A:ASN195 2.1 13.6 1.0 O A:HOH482 2.2 13.2 1.0 CG A:ASN195 3.0 12.6 1.0 CG A:ASP208 3.1 11.3 1.0 ND2 A:ASN195 3.3 10.3 1.0 PB A:ADP303 3.4 13.1 1.0 PA A:ADP303 3.4 12.3 1.0 MG A:MG302 3.6 3.0 1.0 CB A:ASP208 3.6 10.6 1.0 O A:HOH423 3.6 8.0 1.0 O1B A:ADP303 3.7 11.6 1.0 O3A A:ADP303 3.8 12.9 1.0 OG A:SER194 4.1 27.7 1.0 OD1 A:ASP208 4.2 15.8 1.0 OE2 A:GLU24 4.2 42.7 1.0 OD2 A:ASP190 4.2 15.6 1.0 O1A A:ADP303 4.4 12.8 1.0 O5' A:ADP303 4.4 10.3 1.0 CB A:ASN195 4.4 13.6 1.0 O3' A:ADP303 4.5 11.8 1.0 O2B A:ADP303 4.5 12.0 1.0 O A:SER194 4.5 19.2 1.0 C5' A:ADP303 4.5 11.2 1.0 O A:HOH479 4.7 6.2 1.0 C3' A:ADP303 4.8 11.5 1.0 C A:SER194 4.9 19.6 1.0 CA A:ASN195 4.9 17.4 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp 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 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:3.0 occ:1.00 O A:HOH423 1.9 8.0 1.0 O A:HOH483 2.0 10.3 1.0 OD2 A:ASP208 2.0 11.3 1.0 O1B A:ADP303 2.1 11.6 1.0 O A:HOH479 2.1 6.2 1.0 OD1 A:ASP208 2.2 15.8 1.0 CG A:ASP208 2.4 11.3 1.0 PB A:ADP303 3.1 13.1 1.0 O3B A:ADP303 3.2 8.0 1.0 MG A:MG301 3.6 17.9 1.0 OD2 A:ASP190 3.9 15.6 1.0 CB A:ASP208 3.9 10.6 1.0 O A:HOH482 4.1 13.2 1.0 O2B A:ADP303 4.1 12.0 1.0 CB A:SER27 4.1 19.1 1.0 O A:HOH433 4.2 7.2 1.0 NZ A:LYS44 4.2 10.8 1.0 O A:HOH525 4.2 17.1 1.0 O3A A:ADP303 4.3 12.9 1.0 O A:HOH455 4.3 15.0 1.0 OG A:SER27 4.4 14.3 1.0 O A:HOH434 4.4 11.6 1.0 O2A A:ADP303 4.5 11.2 1.0 CA A:ASP208 4.8 10.5 1.0 PA A:ADP303 4.9 12.3 1.0 ND2 A:ASN195 4.9 10.3 1.0 CG A:ASP190 4.9 17.9 1.0 NH2 A:ARG211 4.9 30.0 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp 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 Adp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:16.4 occ:1.00 O B:HOH467 2.0 9.0 1.0 O3B B:ADP304 2.0 11.1 1.0 O2A B:ADP304 2.0 14.1 1.0 OD2 B:ASP208 2.1 15.2 1.0 O B:HOH402 2.1 6.3 1.0 OD1 B:ASN195 2.2 13.1 1.0 CG B:ASP208 3.1 14.1 1.0 CG B:ASN195 3.2 14.6 1.0 PB B:ADP304 3.3 12.5 1.0 PA B:ADP304 3.3 14.6 1.0 ND2 B:ASN195 3.5 13.4 1.0 CB B:ASP208 3.6 10.6 1.0 O1B B:ADP304 3.7 12.9 1.0 O3A B:ADP304 3.7 13.0 1.0 MG B:MG302 3.8 8.3 1.0 O B:HOH451 3.8 22.3 1.0 OE2 B:GLU24 3.9 35.5 1.0 OD1 B:ASP208 4.1 12.2 1.0 OD2 B:ASP190 4.3 14.6 1.0 O5' B:ADP304 4.4 13.3 1.0 O1A B:ADP304 4.4 14.6 1.0 C5' B:ADP304 4.4 12.9 1.0 O3' B:ADP304 4.4 16.7 1.0 O2B B:ADP304 4.4 14.9 1.0 CB B:ASN195 4.6 14.5 1.0 O B:HOH452 4.6 11.2 1.0 O B:SER194 4.7 14.7 1.0 CB B:SER194 4.7 19.3 1.0 C3' B:ADP304 4.7 12.5 1.0 C B:SER194 4.9 16.7 1.0 CD B:GLU24 4.9 36.6 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp 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 Adp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg302 b:8.3 occ:1.00 O B:HOH465 1.9 12.9 1.0 O1B B:ADP304 2.0 12.9 1.0 O B:HOH452 2.0 11.2 1.0 O B:HOH451 2.0 22.3 1.0 OD2 B:ASP208 2.2 15.2 1.0 OD1 B:ASP208 2.3 12.2 1.0 CG B:ASP208 2.5 14.1 1.0 PB B:ADP304 3.1 12.5 1.0 O3B B:ADP304 3.3 11.1 1.0 O B:HOH597 3.5 25.2 1.0 MG B:MG301 3.8 16.4 1.0 O B:HOH402 3.9 6.3 1.0 O B:HOH450 4.0 5.0 1.0 OD2 B:ASP190 4.0 14.6 1.0 O2B B:ADP304 4.0 14.9 1.0 CB B:ASP208 4.1 10.6 1.0 O B:HOH416 4.1 6.5 1.0 CB B:SER27 4.1 21.4 1.0 O B:HOH486 4.2 12.9 1.0 OG B:SER27 4.2 19.8 1.0 NZ B:LYS44 4.2 12.6 1.0 O B:HOH425 4.3 11.0 1.0 O3A B:ADP304 4.3 13.0 1.0 O2A B:ADP304 4.6 14.1 1.0 CA B:ASP208 4.9 9.4 1.0 PA B:ADP304 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