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Magnesium in PDB 1oha: Acetylglutamate Kinase From Escherichia Coli Complexed with Mgadp and N-Acetyl-L-Glutamate

Enzymatic activity of Acetylglutamate Kinase From Escherichia Coli Complexed with Mgadp and N-Acetyl-L-Glutamate

All present enzymatic activity of Acetylglutamate Kinase From Escherichia Coli Complexed with Mgadp and N-Acetyl-L-Glutamate:
2.7.2.8;

Protein crystallography data

The structure of Acetylglutamate Kinase From Escherichia Coli Complexed with Mgadp and N-Acetyl-L-Glutamate, PDB code: 1oha was solved by F.Gil-Ortiz, S.Ramon-Maiques, I.Fita, V.Rubio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.43 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 60.126, 71.792, 107.175, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 23

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Acetylglutamate Kinase From Escherichia Coli Complexed with Mgadp and N-Acetyl-L-Glutamate (pdb code 1oha). 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 Acetylglutamate Kinase From Escherichia Coli Complexed with Mgadp and N-Acetyl-L-Glutamate, PDB code: 1oha:

Magnesium binding site 1 out of 1 in 1oha

Go back to Magnesium Binding Sites List in 1oha
Magnesium binding site 1 out of 1 in the Acetylglutamate Kinase From Escherichia Coli Complexed with Mgadp and N-Acetyl-L-Glutamate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Acetylglutamate Kinase From Escherichia Coli Complexed with Mgadp and N-Acetyl-L-Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1262

b:23.6
occ:1.00
 O A:HOH2138 2.0 23.3 1.0
O1B A:ADP1259 2.0 28.5 1.0
O2A A:ADP1259 2.1 27.5 1.0
O A:HOH2090 2.1 22.4 1.0
O A:HOH2137 2.1 21.6 1.0
O A:HOH2139 2.3 16.6 1.0
PB A:ADP1259 3.1 29.1 1.0
PA A:ADP1259 3.2 28.2 1.0
O3A A:ADP1259 3.5 27.0 1.0
O3B A:ADP1259 3.8 27.7 1.0
OD2 A:ASP162 4.0 18.9 1.0
O5' A:ADP1259 4.1 29.2 1.0
OE1 A:NLG1260 4.1 18.2 1.0
O A:HOH2135 4.2 20.1 1.0
NZ A:LYS217 4.2 19.4 1.0
ND2 A:ASN160 4.2 20.8 1.0
O1A A:ADP1259 4.3 25.9 1.0
O A:HOH2140 4.4 39.0 1.0
OE2 A:NLG1260 4.4 17.5 1.0
OD1 A:ASN160 4.4 20.8 1.0
O2B A:ADP1259 4.4 29.9 1.0
CA A:GLY213 4.6 28.2 1.0
O A:GLY213 4.6 24.5 1.0
NZ A:LYS8 4.6 17.2 1.0
CD A:NLG1260 4.6 16.8 1.0
CG A:ASN160 4.7 19.4 1.0
CG A:ASP162 4.8 18.4 1.0
C A:GLY213 5.0 26.2 1.0

Reference:

F.Gil-Ortiz, S.Ramon-Maiques, I.Fita, V.Rubio. The Course of Phosphorus in the Reaction of N-Acetyl-L-Glutamate Kinase, Determined From the Structures of Crystalline Complexes, Including A Complex with An Alf(4)(-) Transition State Mimic J.Mol.Biol. V. 331 231 2003.
ISSN: ISSN 0022-2836
PubMed: 12875848
DOI: 10.1016/S0022-2836(03)00716-2
Page generated: Tue Aug 13 10:38:52 2024

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