Magnesium in PDB 4ukd: Ump/Cmp Kinase From Slime Mold Complexed with Adp, Udp, Beryllium Fluoride

Enzymatic activity of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Udp, Beryllium Fluoride

All present enzymatic activity of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Udp, Beryllium Fluoride:
2.7.4.14;

Protein crystallography data

The structure of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Udp, Beryllium Fluoride, PDB code: 4ukd was solved by I.Schlichting, J.Reinstein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.00 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.100, 78.100, 101.900, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 21.2

Other elements in 4ukd:

The structure of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Udp, Beryllium Fluoride also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Ump/Cmp Kinase From Slime Mold Complexed with Adp, Udp, Beryllium Fluoride (pdb code 4ukd). 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 Complexed with Adp, Udp, Beryllium Fluoride, PDB code: 4ukd:

Magnesium binding site 1 out of 1 in 4ukd

Go back to Magnesium Binding Sites List in 4ukd
Magnesium binding site 1 out of 1 in the Ump/Cmp Kinase From Slime Mold Complexed with Adp, Udp, Beryllium Fluoride


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 Complexed with Adp, Udp, Beryllium Fluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg500

b:18.4
occ:1.00
 F2 A:BF2501 2.0 19.7 1.0
O A:HOH220 2.2 18.4 1.0
O A:HOH198 2.2 21.8 1.0
O2B A:ADP195 2.3 18.8 1.0
O A:HOH215 2.4 17.2 1.0
O A:HOH900 2.4 17.8 1.0
BE A:BF2501 3.2 19.4 1.0
O3B A:ADP195 3.3 17.1 1.0
PB A:ADP195 3.3 18.0 1.0
O1A A:UDP196 4.0 21.8 1.0
O3B A:UDP196 4.0 19.5 1.0
O2A A:UDP196 4.1 18.9 1.0
OD2 A:ASP89 4.3 18.9 1.0
O A:HOH227 4.3 21.9 1.0
N A:GLY20 4.3 14.8 1.0
F1 A:BF2501 4.3 15.2 1.0
PA A:UDP196 4.3 21.1 1.0
O1B A:ADP195 4.4 19.2 1.0
OD1 A:ASP89 4.4 18.6 1.0
O3A A:ADP195 4.4 19.2 1.0
NH1 A:ARG137 4.4 27.1 1.0
O2A A:ADP195 4.4 17.3 1.0
O3A A:UDP196 4.4 20.3 1.0
OG A:SER36 4.6 18.0 1.0
CA A:GLY20 4.6 16.2 1.0
O A:HOH208 4.6 15.8 1.0
O A:HOH553 4.6 29.4 1.0
NH1 A:ARG131 4.8 22.9 1.0
CG A:ASP89 4.8 19.2 1.0
CE A:LYS19 4.8 12.8 1.0
PB A:UDP196 4.8 20.8 1.0
O A:HOH664 4.9 50.0 1.0
NZ A:LYS19 4.9 12.8 1.0
PA A:ADP195 4.9 18.8 1.0
CB A:LYS19 5.0 15.0 1.0

Reference:

I.Schlichting, J.Reinstein. Structures of Active Conformations of Ump Kinase From Dictyostelium Discoideum Suggest Phosphoryl Transfer Is Associative. Biochemistry V. 36 9290 1997.
ISSN: ISSN 0006-2960
PubMed: 9280438
DOI: 10.1021/BI970974C
Page generated: Mon Dec 14 19:37:22 2020

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