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Magnesium in PDB 1p18: Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex

Enzymatic activity of Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex

All present enzymatic activity of Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex:
2.4.2.8;

Protein crystallography data

The structure of Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex, PDB code: 1p18 was solved by B.Canyuk, A.E.Eakin, S.P.Craig Iii, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.500, 102.100, 51.800, 90.00, 94.30, 90.00
R / Rfree (%) 21 / 29.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex (pdb code 1p18). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex, PDB code: 1p18:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1p18

Go back to Magnesium Binding Sites List in 1p18
Magnesium binding site 1 out of 4 in the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg900

b:62.7
occ:1.00
 O A:HOH6402 2.0 44.7 1.0
O3 A:PRP801 2.0 72.1 1.0
O2 A:PRP801 2.2 66.7 1.0
O A:HOH6403 2.3 49.3 1.0
OE2 A:GLU111 2.5 45.7 1.0
C3 A:PRP801 2.6 74.5 1.0
C2 A:PRP801 2.6 71.4 1.0
O3B A:PRP801 2.7 49.4 1.0
O1 A:PRP801 2.7 64.1 1.0
OD1 A:ASP112 2.9 38.7 1.0
C1 A:PRP801 3.2 69.7 1.0
CD A:GLU111 3.4 41.6 1.0
OE1 A:GLU111 3.4 46.7 1.0
CG A:ASP112 3.8 35.5 1.0
C4 A:PRP801 3.9 79.0 1.0
PB A:PRP801 3.9 44.5 1.0
O3A A:PRP801 3.9 57.5 1.0
OD2 A:ASP112 4.1 36.4 1.0
PA A:PRP801 4.1 61.1 1.0
O4 A:PRP801 4.1 76.0 1.0
O A:VAL50 4.5 30.1 1.0
O A:LEU51 4.5 24.7 1.0
N A:GLY53 4.7 30.4 1.0
OG A:SER54 4.7 31.3 1.0
O2A A:PRP801 4.8 56.6 1.0
O A:HOH6406 4.8 35.6 1.0
O1B A:PRP801 4.8 44.1 1.0
O2B A:PRP801 4.9 50.8 1.0
CG A:GLU111 4.9 35.6 1.0
CA A:GLY53 4.9 30.7 1.0
N A:ASP112 5.0 28.2 1.0
C A:LEU51 5.0 23.3 1.0

Magnesium binding site 2 out of 4 in 1p18

Go back to Magnesium Binding Sites List in 1p18
Magnesium binding site 2 out of 4 in the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg902

b:44.8
occ:1.00
 O A:HOH6404 1.9 36.7 1.0
O2A A:PRP801 2.0 56.6 1.0
OD1 A:ASP171 2.2 36.9 1.0
O A:HOH6406 2.2 35.6 1.0
O1B A:PRP801 2.4 44.1 1.0
O A:HOH6405 2.4 41.2 1.0
CG A:ASP171 3.0 30.2 1.0
OD2 A:ASP171 3.2 34.8 1.0
PA A:PRP801 3.4 61.1 1.0
PB A:PRP801 3.6 44.5 1.0
O A:HOH6201 3.8 71.2 1.0
O3A A:PRP801 3.8 57.5 1.0
O A:ASP171 3.9 23.4 1.0
NH2 A:ARG177 4.2 22.6 1.0
N3 A:7HP800 4.2 53.6 1.0
NH1 A:ARG177 4.2 28.2 1.0
CB A:ASP171 4.3 26.3 1.0
N A:ASP171 4.3 18.3 1.0
O1A A:PRP801 4.3 59.2 1.0
O1 A:PRP801 4.3 64.1 1.0
C1 A:PRP801 4.3 69.7 1.0
C A:ASP171 4.4 28.0 1.0
O2 A:PRP801 4.4 66.7 1.0
O3B A:PRP801 4.5 49.4 1.0
CA A:ASP171 4.6 26.1 1.0
CZ A:ARG177 4.6 26.2 1.0
O2B A:PRP801 4.6 50.8 1.0
C2 A:7HP800 4.8 52.3 1.0

Magnesium binding site 3 out of 4 in 1p18

Go back to Magnesium Binding Sites List in 1p18
Magnesium binding site 3 out of 4 in the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg912

b:26.4
occ:1.00
 O B:HOH6407 1.9 26.2 1.0
O2A B:PRP811 2.1 34.0 1.0
O B:HOH6408 2.2 27.8 1.0
O1B B:PRP811 2.3 25.2 1.0
OD1 B:ASP171 2.3 23.6 1.0
O B:HOH6409 2.3 30.9 1.0
PA B:PRP811 3.2 38.2 1.0
CG B:ASP171 3.3 20.0 1.0
O3A B:PRP811 3.4 40.7 1.0
PB B:PRP811 3.4 28.2 1.0
OD2 B:ASP171 3.6 19.8 1.0
O1 B:PRP811 4.0 31.9 1.0
O B:ASP171 4.1 27.0 1.0
C1 B:PRP811 4.2 37.2 1.0
O B:HOH6400 4.2 27.4 1.0
NH2 B:ARG177 4.3 24.5 1.0
O3B B:PRP811 4.3 23.7 1.0
O B:GLY83 4.4 52.4 1.0
O1A B:PRP811 4.4 40.6 1.0
O2B B:PRP811 4.5 23.2 1.0
N3 B:7HP810 4.5 30.6 1.0
O B:HOH1050 4.6 27.2 1.0
NH1 B:ARG177 4.6 20.6 1.0
O2 B:PRP811 4.6 38.8 1.0
CB B:ASP171 4.7 17.0 1.0
CB B:TYR82 4.7 55.9 1.0
C B:ASP171 4.8 26.2 1.0
CZ B:ARG177 4.8 25.3 1.0
N B:ASP171 4.8 19.6 1.0

Magnesium binding site 4 out of 4 in 1p18

Go back to Magnesium Binding Sites List in 1p18
Magnesium binding site 4 out of 4 in the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, K68R Mutant, Ternary Substrates Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg910

b:36.8
occ:1.00
 O B:HOH6410 2.0 30.4 1.0
O3 B:PRP811 2.1 39.0 1.0
O2 B:PRP811 2.1 38.8 1.0
O B:HOH6411 2.2 27.9 1.0
O3B B:PRP811 2.5 23.7 1.0
O1 B:PRP811 2.6 31.9 1.0
C2 B:PRP811 2.8 37.5 1.0
C3 B:PRP811 2.9 36.3 1.0
C1 B:PRP811 3.2 37.2 1.0
OD1 B:ASP112 3.4 47.2 1.0
OE2 B:GLU111 3.6 29.2 1.0
PB B:PRP811 3.6 28.2 1.0
O3A B:PRP811 3.8 40.7 1.0
PA B:PRP811 3.9 38.2 1.0
C4 B:PRP811 4.1 37.5 1.0
O B:HOH6401 4.1 37.8 1.0
OE1 B:GLU111 4.1 27.2 1.0
O4 B:PRP811 4.2 38.5 1.0
O B:LEU51 4.2 33.7 1.0
CG B:ASP112 4.3 43.0 1.0
OD2 B:ASP112 4.3 46.3 1.0
CD B:GLU111 4.3 25.5 1.0
O B:VAL50 4.4 19.5 1.0
O1B B:PRP811 4.5 25.2 1.0
O2B B:PRP811 4.5 23.2 1.0
CG1 B:VAL50 4.5 19.9 1.0
N B:GLY53 4.6 23.4 1.0
N B:ARG52 4.7 27.0 1.0
C B:LEU51 4.7 28.8 1.0
O1A B:PRP811 4.7 40.6 1.0
O B:HOH6409 4.8 30.9 1.0
O2A B:PRP811 4.9 34.0 1.0
CA B:GLY53 4.9 24.6 1.0

Reference:

B.Canyuk, F.J.Medrano, M.A.Wenck, P.J.Focia, A.E.Eakin, S.P.Craig Iii. Interactions at the Dimer Interface Influence the Relative Efficiencies For Purine Nucleotide Synthesis and Pyrophosphorolysis in A Phosphoribosyltransferase J.Mol.Biol. V. 335 905 2004.
ISSN: ISSN 0022-2836
PubMed: 14698288
DOI: 10.1016/J.JMB.2003.11.012
Page generated: Tue Aug 13 10:46:13 2024

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