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Atomistry » Magnesium » PDB 1g87-1gpm » 1gll » |
Magnesium in PDB 1gll: Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain MotionEnzymatic activity of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion
All present enzymatic activity of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion:
2.7.1.30; Protein crystallography data
The structure of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion, PDB code: 1gll
was solved by
C.E.Bystrom,
D.W.Pettigrew,
B.P.Branchaud,
S.J.Remington,
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 Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion
(pdb code 1gll). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion, PDB code: 1gll: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 1gllGo back to Magnesium Binding Sites List in 1gll
Magnesium binding site 1 out
of 2 in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 1gllGo back to Magnesium Binding Sites List in 1gll
Magnesium binding site 2 out
of 2 in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion
Mono view Stereo pair view
Reference:
C.E.Bystrom,
D.W.Pettigrew,
B.P.Branchaud,
P.O'brien,
S.J.Remington.
Crystal Structures of Escherichia Coli Glycerol Kinase Variant S58-->W in Complex with Nonhydrolyzable Atp Analogues Reveal A Putative Active Conformation of the Enzyme As A Result of Domain Motion. Biochemistry V. 38 3508 1999.
Page generated: Mon Dec 14 05:58:03 2020
ISSN: ISSN 0006-2960 PubMed: 10090737 DOI: 10.1021/BI982460Z |
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