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Atomistry » Magnesium » PDB 1gq9-1h7q » 1gs5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 1gq9-1h7q » 1gs5 » |
Magnesium in PDB 1gs5: N-Acetyl-L-Glutamate Kinase From Escherichia Coli Complexed with Its Substrate N-Acetylglutamate and Its Substrate Analog AmppnpEnzymatic 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:
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 1gs5Go back to![]() ![]()
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
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.
Page generated: Tue Aug 13 03:50:42 2024
ISSN: ISSN 0969-2126 PubMed: 12005432 DOI: 10.1016/S0969-2126(02)00721-9 |
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