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Magnesium in PDB 1l8t: Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Kanamycin A Complex

Enzymatic activity of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Kanamycin A Complex

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

Protein crystallography data

The structure of Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Kanamycin A Complex, PDB code: 1l8t 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) 40.00 / 2.40
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 46.629, 46.629, 301.289, 90.00, 90.00, 90.00
R / Rfree (%) 23.4 / 29.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Kanamycin A Complex (pdb code 1l8t). 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 Kanamycin A Complex, PDB code: 1l8t:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1l8t

Go back to Magnesium Binding Sites List in 1l8t
Magnesium binding site 1 out of 2 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Kanamycin A 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 Kanamycin A Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:39.5
occ:1.00
O2A A:ADP300 1.8 26.3 1.0
O A:HOH526 1.8 22.0 1.0
OD1 A:ASN195 1.9 39.9 1.0
OD2 A:ASP208 2.0 32.9 1.0
O A:HOH528 2.0 28.9 1.0
O3B A:ADP300 2.1 29.1 1.0
CG A:ASN195 2.9 38.5 1.0
CG A:ASP208 3.1 32.6 1.0
PA A:ADP300 3.2 33.8 1.0
ND2 A:ASN195 3.3 38.3 1.0
PB A:ADP300 3.4 29.4 1.0
O3A A:ADP300 3.6 31.1 1.0
CB A:ASP208 3.7 32.3 1.0
O1B A:ADP300 3.8 27.6 1.0
O A:HOH527 3.8 18.1 1.0
OG A:SER194 4.0 42.0 1.0
O A:HOH564 4.0 32.5 1.0
MG A:MG302 4.1 33.9 1.0
OD1 A:ASP208 4.1 32.6 1.0
O1A A:ADP300 4.1 30.6 1.0
O A:SER194 4.2 36.2 1.0
O5' A:ADP300 4.2 33.4 1.0
CB A:ASN195 4.2 38.7 1.0
C5' A:ADP300 4.4 33.6 1.0
O A:HOH539 4.4 23.2 1.0
O7 A:KAN1 4.5 45.6 1.0
O2B A:ADP300 4.5 28.9 1.0
OD2 A:ASP190 4.5 31.7 1.0
C A:SER194 4.5 37.0 1.0
O3' A:ADP300 4.6 31.2 1.0
CA A:ASN195 4.7 38.5 1.0
CB A:SER194 4.7 38.2 1.0
C3' A:ADP300 4.7 33.5 1.0
N A:ASN195 4.8 37.5 1.0

Magnesium binding site 2 out of 2 in 1l8t

Go back to Magnesium Binding Sites List in 1l8t
Magnesium binding site 2 out of 2 in the Crystal Structure of 3',5"-Aminoglycoside Phosphotransferase Type Iiia Adp Kanamycin A 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 Kanamycin A Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg302

b:33.9
occ:1.00
O A:HOH539 1.8 23.2 1.0
O1B A:ADP300 2.0 27.6 1.0
O A:HOH527 2.0 18.1 1.0
O A:HOH562 2.0 29.1 1.0
OD1 A:ASP208 2.2 32.6 1.0
OD2 A:ASP208 2.6 32.9 1.0
CG A:ASP208 2.7 32.6 1.0
PB A:ADP300 3.1 29.4 1.0
O3B A:ADP300 3.3 29.1 1.0
O A:HOH528 3.8 28.9 1.0
O A:HOH555 3.8 34.8 1.0
O A:HOH552 3.9 39.2 1.0
CB A:SER27 3.9 37.7 1.0
O A:HOH525 3.9 22.9 1.0
O8 A:KAN1 3.9 44.6 1.0
OD2 A:ASP190 4.0 31.7 1.0
O2B A:ADP300 4.0 28.9 1.0
O7 A:KAN1 4.0 45.6 1.0
MG A:MG301 4.1 39.5 1.0
O A:HOH544 4.1 24.5 1.0
CB A:ASP208 4.2 32.3 1.0
NZ A:LYS44 4.2 38.5 1.0
OG A:SER27 4.2 34.2 1.0
O3A A:ADP300 4.3 31.1 1.0
O A:HOH564 4.5 32.5 1.0
O2A A:ADP300 4.7 26.3 1.0
C4 A:KAN1 4.9 42.8 1.0
CA A:ASP208 4.9 30.9 1.0
PA A:ADP300 5.0 33.8 1.0
C3 A:KAN1 5.0 42.9 1.0

Reference:

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
Page generated: Sun Aug 10 00:38:59 2025

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