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Magnesium in PDB 1b8o: Purine Nucleoside Phosphorylase

Enzymatic activity of Purine Nucleoside Phosphorylase

All present enzymatic activity of Purine Nucleoside Phosphorylase:
2.4.2.1;

Protein crystallography data

The structure of Purine Nucleoside Phosphorylase, PDB code: 1b8o was solved by A.A.Fedorov, G.A.Kicska, E.V.Fedorov, W.Shi, P.C.Tyler, R.H.Furneaux, V.L.Schramm, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.50
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 92.683, 92.683, 92.683, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 23.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Purine Nucleoside Phosphorylase (pdb code 1b8o). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Purine Nucleoside Phosphorylase, PDB code: 1b8o:

Magnesium binding site 1 out of 1 in 1b8o

Go back to Magnesium Binding Sites List in 1b8o
Magnesium binding site 1 out of 1 in the Purine Nucleoside Phosphorylase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Purine Nucleoside Phosphorylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg598

b:15.1
occ:1.00
O A:HOH326 2.2 11.6 1.0
O A:HOH328 2.3 13.5 1.0
O A:HOH319 2.3 14.2 1.0
O A:HOH329 2.3 13.6 1.0
O A:HOH342 2.3 14.3 1.0
O A:HOH348 2.3 16.6 1.0
OE2 A:GLU22 4.1 12.8 1.0
OE1 A:GLU22 4.1 14.2 1.0
O A:ALA45 4.3 14.7 1.0
O A:HOH362 4.3 17.5 1.0
O A:HOH465 4.3 31.2 1.0
O A:GLN44 4.4 14.6 1.0
OE1 A:GLN46 4.4 12.6 1.0
CD A:GLU22 4.5 13.4 1.0
CB A:GLN46 4.6 11.2 1.0
C A:GLN44 4.8 14.9 1.0
C A:ALA45 4.9 13.6 1.0
CD A:GLN46 5.0 11.1 1.0

Reference:

A.Fedorov, W.Shi, G.Kicska, E.Fedorov, P.C.Tyler, R.H.Furneaux, J.C.Hanson, G.J.Gainsford, J.Z.Larese, V.L.Schramm, S.C.Almo. Transition State Structure of Purine Nucleoside Phosphorylase and Principles of Atomic Motion in Enzymatic Catalysis. Biochemistry V. 40 853 2001.
ISSN: ISSN 0006-2960
PubMed: 11170405
DOI: 10.1021/BI002499F
Page generated: Sat Aug 9 20:11:31 2025

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