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Manganese in PDB 1tc2: Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi

Enzymatic activity of Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi

All present enzymatic activity of Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi:
2.4.2.8;

Protein crystallography data

The structure of Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, PDB code: 1tc2 was solved by P.J.Focia, S.P.Craig Iii, A.E.Eakin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 1.81
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 39.420, 101.760, 51.920, 90.00, 94.23, 90.00
R / Rfree (%) 18.3 / 23.2

Other elements in 1tc2:

The structure of Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi (pdb code 1tc2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi, PDB code: 1tc2:

Manganese binding site 1 out of 1 in 1tc2

Go back to Manganese Binding Sites List in 1tc2
Manganese binding site 1 out of 1 in the Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Ternary Substrate Complex of the Hypoxanthine Phosphoribosyltransferase From Trypanosoma Cruzi within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn910

b:17.3
occ:1.00
O B:HOH1290 2.1 13.3 1.0
O B:HOH1291 2.1 13.8 1.0
O3B B:PRP811 2.2 13.6 1.0
O2 B:PRP811 2.3 15.9 1.0
O3 B:PRP811 2.3 16.6 1.0
O1 B:PRP811 2.6 16.5 1.0
C2 B:PRP811 3.1 14.6 1.0
C3 B:PRP811 3.2 13.3 1.0
PB B:PRP811 3.3 15.0 1.0
O3A B:PRP811 3.3 16.7 1.0
C1 B:PRP811 3.4 14.3 1.0
PA B:PRP811 3.7 16.3 1.0
OD1 B:ASP612 3.9 15.4 1.0
OE2 B:GLU611 3.9 18.6 1.0
OE1 B:GLU611 4.0 17.4 1.0
O1B B:PRP811 4.1 16.1 1.0
O B:HOH1027 4.1 20.5 1.0
C4 B:PRP811 4.2 13.5 1.0
N B:GLY553 4.2 16.9 1.0
O4 B:PRP811 4.2 12.6 1.0
O B:VAL550 4.3 12.4 1.0
O2B B:PRP811 4.3 14.5 1.0
O B:LEU551 4.4 15.8 1.0
CD B:GLU611 4.4 17.2 1.0
O B:HOH1031 4.4 24.6 1.0
CA B:GLY553 4.5 17.2 1.0
CG1 B:VAL550 4.5 13.9 1.0
O1A B:PRP811 4.5 17.0 1.0
O B:VAL579 4.6 17.9 1.0
N B:LYS552 4.7 15.1 1.0
O2A B:PRP811 4.7 12.5 1.0
C B:LEU551 4.7 16.0 1.0
CG B:ASP612 4.7 14.2 1.0
OD2 B:ASP612 4.8 17.4 1.0
O B:HOH1289 5.0 17.2 1.0

Reference:

P.J.Focia, S.P.Craig Iii, A.E.Eakin. Approaching the Transition State in the Crystal Structure of A Phosphoribosyltransferase. Biochemistry V. 37 17120 1998.
ISSN: ISSN 0006-2960
PubMed: 9860824
DOI: 10.1021/BI9821465
Page generated: Sat Oct 5 12:33:31 2024

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