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Aluminium in PDB 3ukd: Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3

Enzymatic activity of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3

All present enzymatic activity of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3:
2.7.4.14;

Protein crystallography data

The structure of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3, PDB code: 3ukd 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) 9.90 / 1.90
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.800, 78.800, 100.700, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 23.2

Other elements in 3ukd:

The structure of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3 also contains other interesting chemical elements:

Fluorine (F) 3 atoms
Magnesium (Mg) 1 atom

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3 (pdb code 3ukd). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3, PDB code: 3ukd:

Aluminium binding site 1 out of 1 in 3ukd

Go back to Aluminium Binding Sites List in 3ukd
Aluminium binding site 1 out of 1 in the Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Ump/Cmp Kinase From Slime Mold Complexed with Adp, Cmp, and ALF3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al501

b:27.3
occ:1.00
AL A:AF3501 0.0 27.3 1.0
F3 A:AF3501 1.6 25.6 1.0
F2 A:AF3501 1.7 28.9 1.0
F1 A:AF3501 1.7 25.1 1.0
O3B A:ADP195 2.0 14.8 1.0
O3P A:C5P196 2.2 17.6 1.0
PB A:ADP195 3.4 17.0 1.0
NH2 A:ARG148 3.4 21.1 1.0
P A:C5P196 3.4 18.8 1.0
O A:HOH198 3.5 24.1 1.0
MG A:MG500 3.6 19.8 1.0
O2B A:ADP195 3.6 17.1 1.0
O2P A:C5P196 3.7 18.1 1.0
NH1 A:ARG137 3.8 23.8 1.0
NH1 A:ARG148 3.8 21.6 1.0
NH2 A:ARG137 4.0 19.9 1.0
NH1 A:ARG131 4.0 19.1 1.0
N A:GLY16 4.0 14.8 1.0
O1B A:ADP195 4.0 18.0 1.0
O1P A:C5P196 4.1 18.6 1.0
CZ A:ARG148 4.1 22.6 1.0
NZ A:LYS19 4.1 14.5 1.0
NH2 A:ARG131 4.3 19.3 1.0
CZ A:ARG137 4.4 23.0 1.0
CA A:PRO15 4.4 18.2 1.0
NH2 A:ARG93 4.4 19.5 1.0
O3A A:ADP195 4.4 18.3 1.0
O A:HOH215 4.5 13.7 1.0
O5' A:C5P196 4.6 15.8 1.0
CZ A:ARG131 4.6 21.9 1.0
O A:HOH220 4.7 21.8 1.0
C A:PRO15 4.7 17.7 1.0
CE A:LYS19 4.8 15.6 1.0
CA A:GLY16 4.8 15.2 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: Sun Jul 6 21:50:15 2025

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