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Magnesium in PDB 2j5v: Glutamate 5-Kinase From Escherichia Coli Complexed with Glutamyl-5-Phosphate and Pyroglutamic Acid

Enzymatic activity of Glutamate 5-Kinase From Escherichia Coli Complexed with Glutamyl-5-Phosphate and Pyroglutamic Acid

All present enzymatic activity of Glutamate 5-Kinase From Escherichia Coli Complexed with Glutamyl-5-Phosphate and Pyroglutamic Acid:
2.7.2.11;

Protein crystallography data

The structure of Glutamate 5-Kinase From Escherichia Coli Complexed with Glutamyl-5-Phosphate and Pyroglutamic Acid, PDB code: 2j5v was solved by C.Marco-Marin, F.Gil-Ortiz, I.Perez-Arellano, J.Cervera, I.Fita, V.Rubio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 88.39 / 2.5
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 101.455, 101.455, 178.728, 90.00, 90.00, 90.00
R / Rfree (%) 19.2 / 24.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Glutamate 5-Kinase From Escherichia Coli Complexed with Glutamyl-5-Phosphate and Pyroglutamic Acid (pdb code 2j5v). 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 Glutamate 5-Kinase From Escherichia Coli Complexed with Glutamyl-5-Phosphate and Pyroglutamic Acid, PDB code: 2j5v:

Magnesium binding site 1 out of 1 in 2j5v

Go back to Magnesium Binding Sites List in 2j5v
Magnesium binding site 1 out of 1 in the Glutamate 5-Kinase From Escherichia Coli Complexed with Glutamyl-5-Phosphate and Pyroglutamic Acid


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Glutamate 5-Kinase From Escherichia Coli Complexed with Glutamyl-5-Phosphate and Pyroglutamic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1368

b:19.3
occ:0.60
 O A:LEU168 2.3 40.5 1.0
O2 A:SO41371 2.4 53.7 0.7
NZ A:LYS10 2.8 33.7 1.0
O1 A:SO41371 3.0 52.6 0.7
N A:GLY12 3.1 35.7 1.0
S A:SO41371 3.2 54.5 0.7
CA A:GLY12 3.5 35.4 1.0
C A:LEU168 3.5 40.6 1.0
CE A:LYS10 3.7 33.5 1.0
O4 A:SO41371 3.8 54.5 0.7
CD A:LYS10 3.8 33.7 1.0
CG2 A:VAL15 3.9 37.8 1.0
O A:HOH2088 4.0 42.9 1.0
CE A:LYS217 4.1 44.9 1.0
OA2 A:RGP1370 4.1 47.6 0.6
NZ A:LYS217 4.2 46.6 1.0
C A:LEU11 4.3 35.7 1.0
CA A:THR169 4.3 44.0 1.0
N A:THR169 4.4 42.1 1.0
O3 A:SO41371 4.4 53.0 0.7
C A:GLY12 4.4 35.8 1.0
O A:LYS10 4.5 34.8 1.0
CA A:LEU11 4.6 35.7 1.0
CA A:LEU168 4.6 39.1 1.0
OD1 A:ASP150 4.6 30.5 1.0
N A:LEU168 4.7 37.5 1.0
O A:GLY12 4.7 35.9 1.0
CB A:VAL15 4.7 38.7 1.0

Reference:

C.Marco-Marin, F.Gil-Ortiz, I.Perez-Arellano, J.Cervera, I.Fita, V.Rubio. A Novel Two-Domain Architecture Within the Amino Acid Kinase Enzyme Family Revealed By the Crystal Structure of Escherichia Coli Glutamate 5-Kinase. J.Mol.Biol. V. 367 1431 2007.
ISSN: ISSN 0022-2836
PubMed: 17321544
DOI: 10.1016/J.JMB.2007.01.073
Page generated: Mon Dec 14 07:28:32 2020

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