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Atomistry » Arsenic » PDB 1glj-1pqu » 1glj | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Arsenic » PDB 1glj-1pqu » 1glj » |
Arsenic in PDB 1glj: 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: 1glj
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:
Other elements in 1glj:
The structure of Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion also contains other interesting chemical elements:
Arsenic Binding Sites:
The binding sites of Arsenic atom in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion
(pdb code 1glj). This binding sites where shown within
5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Escherichia Coli Glycerol Kinase Mutant with Bound Atp Analog Showing Substantial Domain Motion, PDB code: 1glj: Jump to Arsenic binding site number: 1; 2; Arsenic binding site 1 out of 2 in 1gljGo back to![]() ![]()
Arsenic 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
Arsenic binding site 2 out of 2 in 1gljGo back to![]() ![]()
Arsenic 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: Sun Jul 6 22:55:09 2025
ISSN: ISSN 0006-2960 PubMed: 10090737 DOI: 10.1021/BI982460Z |
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