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Magnesium in PDB 1uke: Ump/Cmp Kinase From Slime Mold

Enzymatic activity of Ump/Cmp Kinase From Slime Mold

All present enzymatic activity of Ump/Cmp Kinase From Slime Mold:
2.7.4.14;

Protein crystallography data

The structure of Ump/Cmp Kinase From Slime Mold, PDB code: 1uke was solved by K.Scheffzek, W.Kliche, L.Wiesmueller, J.Reinstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.20
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.500, 78.500, 101.500, 90.00, 90.00, 90.00
R / Rfree (%) 21.5 / 27.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Ump/Cmp Kinase From Slime Mold (pdb code 1uke). 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 Ump/Cmp Kinase From Slime Mold, PDB code: 1uke:

Magnesium binding site 1 out of 1 in 1uke

Go back to Magnesium Binding Sites List in 1uke
Magnesium binding site 1 out of 1 in the Ump/Cmp Kinase From Slime Mold


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ump/Cmp Kinase From Slime Mold within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg196

b:11.5
occ:1.00
H1 A:HOH215 1.7 0.0 1.0
H1 A:HOH220 1.9 0.0 1.0
O2G A:UP5195 2.3 17.4 1.0
O2B A:UP5195 2.3 14.1 1.0
O A:HOH198 2.3 14.3 1.0
O A:HOH215 2.3 18.8 1.0
O A:HOH227 2.3 26.4 1.0
O A:HOH220 2.4 16.1 1.0
H2 A:HOH215 2.5 0.0 1.0
H2 A:HOH227 2.5 0.0 1.0
H2 A:HOH198 2.8 0.0 1.0
H1 A:HOH227 2.9 0.0 1.0
H1 A:HOH198 2.9 0.0 1.0
H2 A:HOH220 3.0 0.0 1.0
PG A:UP5195 3.5 15.0 1.0
PB A:UP5195 3.5 14.6 1.0
H2 A:HOH197 3.7 0.0 1.0
H A:GLY20 3.7 0.0 1.0
O3B A:UP5195 3.7 15.3 1.0
HG A:SER36 3.7 0.0 1.0
HH12 A:ARG137 3.9 0.0 1.0
O1E A:UP5195 4.1 10.5 1.0
OD2 A:ASP89 4.1 15.9 1.0
O2E A:UP5195 4.2 18.6 1.0
O A:HOH197 4.2 25.3 1.0
OD1 A:ASP89 4.2 17.7 1.0
OG A:SER36 4.2 18.4 1.0
N A:GLY20 4.3 12.1 1.0
O2A A:UP5195 4.4 13.6 1.0
CA A:GLY20 4.4 7.7 1.0
H2 A:HOH208 4.4 0.0 1.0
O3G A:UP5195 4.5 18.5 1.0
O1B A:UP5195 4.5 10.1 1.0
PE A:UP5195 4.5 16.8 1.0
O1G A:UP5195 4.5 20.5 1.0
O3A A:UP5195 4.5 16.7 1.0
HZ2 A:LYS19 4.6 0.0 1.0
O3D A:UP5195 4.6 17.6 1.0
O1D A:UP5195 4.6 16.9 1.0
CG A:ASP89 4.6 17.8 1.0
H1 A:HOH197 4.7 0.0 1.0
O A:HOH208 4.8 25.4 1.0
CE A:LYS19 4.9 9.7 1.0
NH1 A:ARG137 4.9 54.4 1.0
PD A:UP5195 4.9 18.0 1.0
HH12 A:ARG131 5.0 0.0 1.0
PA A:UP5195 5.0 14.4 1.0

Reference:

K.Scheffzek, W.Kliche, L.Wiesmuller, J.Reinstein. Crystal Structure of the Complex of Ump/Cmp Kinase From Dictyostelium Discoideum and the Bisubstrate Inhibitor P1-(5'-Adenosyl) P5-(5'-Uridyl) Pentaphosphate (UP5A) and MG2+ at 2.2 A: Implications For Water-Mediated Specificity. Biochemistry V. 35 9716 1996.
ISSN: ISSN 0006-2960
PubMed: 8703943
DOI: 10.1021/BI960642S
Page generated: Mon Dec 14 06:53:11 2020

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