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Magnesium in PDB 1gs5: N-Acetyl-L-Glutamate Kinase From Escherichia Coli Complexed with Its Substrate N-Acetylglutamate and Its Substrate Analog Amppnp

Enzymatic activity of N-Acetyl-L-Glutamate Kinase From Escherichia Coli Complexed with Its Substrate N-Acetylglutamate and Its Substrate Analog Amppnp

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

Protein crystallography data

The structure of N-Acetyl-L-Glutamate Kinase From Escherichia Coli Complexed with Its Substrate N-Acetylglutamate and Its Substrate Analog Amppnp, PDB code: 1gs5 was solved by S.Ramon-Maiques, A.Marina, F.Gil-Ortiz, I.Fita, V.Rubio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50 / 1.5
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 59.564, 72.332, 107.418, 90.00, 90.00, 90.00
R / Rfree (%) 20.88 / 21.28

Magnesium Binding Sites:

The binding sites of Magnesium atom in the N-Acetyl-L-Glutamate Kinase From Escherichia Coli Complexed with Its Substrate N-Acetylglutamate and Its Substrate Analog Amppnp (pdb code 1gs5). 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 N-Acetyl-L-Glutamate Kinase From Escherichia Coli Complexed with Its Substrate N-Acetylglutamate and Its Substrate Analog Amppnp, PDB code: 1gs5:

Magnesium binding site 1 out of 1 in 1gs5

Go back to Magnesium Binding Sites List in 1gs5
Magnesium binding site 1 out of 1 in the N-Acetyl-L-Glutamate Kinase From Escherichia Coli Complexed with Its Substrate N-Acetylglutamate and Its Substrate Analog Amppnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of N-Acetyl-L-Glutamate Kinase From Escherichia Coli Complexed with Its Substrate N-Acetylglutamate and Its Substrate Analog Amppnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1261

b:39.0
occ:1.00
 O2A A:ANP1260 2.1 54.1 0.7
O1B A:ANP1260 2.2 32.2 0.7
O A:HOH2195 2.5 27.1 1.0
O A:HOH2135 2.6 32.0 1.0
O2G A:ANP1260 2.8 38.2 0.7
PB A:ANP1260 3.2 40.4 0.7
PA A:ANP1260 3.2 48.3 0.7
O3A A:ANP1260 3.6 48.7 0.7
N3B A:ANP1260 3.6 35.3 0.7
PG A:ANP1260 3.7 40.3 0.7
OD2 A:ASP162 3.9 22.7 1.0
ND2 A:ASN160 3.9 25.8 1.0
O1G A:ANP1260 4.0 30.0 0.7
OE1 A:NLG1259 4.1 22.4 1.0
O5' A:ANP1260 4.2 29.1 0.7
NZ A:LYS217 4.3 32.8 1.0
O A:HOH2196 4.4 43.2 1.0
O1A A:ANP1260 4.5 55.2 0.7
OE2 A:NLG1259 4.5 30.0 1.0
NZ A:LYS8 4.5 20.9 1.0
O2B A:ANP1260 4.5 48.1 0.7
O A:HOH2194 4.6 31.4 1.0
CG A:ASP162 4.7 22.8 1.0
CD A:NLG1259 4.7 21.7 1.0
CG A:ASN160 4.9 20.7 1.0

Reference:

S.Ramon-Maiques, A.Marina, F.Gil-Ortiz, I.Fita, V.Rubio. Structure of Acetylglutamate Kinase, A Key Enzyme For Arginine Biosynthesis and A Prototype For the Amino Acid Kinase Enzyme Family, During Catalysis Structure V. 10 329 2002.
ISSN: ISSN 0969-2126
PubMed: 12005432
DOI: 10.1016/S0969-2126(02)00721-9
Page generated: Sat Aug 9 21:23:04 2025

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