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Atomistry » Chlorine » PDB 1go6-1hav » 1grg | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 1go6-1hav » 1grg » |
Chlorine in PDB 1grg: Substrate Binding and Catalysis By Glutathione Reductase As Derived From Refined Enzyme: Substrate Crystal Structures at 2 Angstroms ResolutionEnzymatic activity of Substrate Binding and Catalysis By Glutathione Reductase As Derived From Refined Enzyme: Substrate Crystal Structures at 2 Angstroms Resolution
All present enzymatic activity of Substrate Binding and Catalysis By Glutathione Reductase As Derived From Refined Enzyme: Substrate Crystal Structures at 2 Angstroms Resolution:
1.6.4.2; Protein crystallography data
The structure of Substrate Binding and Catalysis By Glutathione Reductase As Derived From Refined Enzyme: Substrate Crystal Structures at 2 Angstroms Resolution, PDB code: 1grg
was solved by
P.A.Karplus,
G.E.Schulz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Substrate Binding and Catalysis By Glutathione Reductase As Derived From Refined Enzyme: Substrate Crystal Structures at 2 Angstroms Resolution
(pdb code 1grg). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Substrate Binding and Catalysis By Glutathione Reductase As Derived From Refined Enzyme: Substrate Crystal Structures at 2 Angstroms Resolution, PDB code: 1grg: Chlorine binding site 1 out of 1 in 1grgGo back to Chlorine Binding Sites List in 1grg
Chlorine binding site 1 out
of 1 in the Substrate Binding and Catalysis By Glutathione Reductase As Derived From Refined Enzyme: Substrate Crystal Structures at 2 Angstroms Resolution
Mono view Stereo pair view
Reference:
P.A.Karplus,
G.E.Schulz.
Substrate Binding and Catalysis By Glutathione Reductase As Derived From Refined Enzyme: Substrate Crystal Structures at 2 A Resolution. J.Mol.Biol. V. 210 163 1989.
Page generated: Sat Dec 12 08:36:15 2020
ISSN: ISSN 0022-2836 PubMed: 2585516 DOI: 10.1016/0022-2836(89)90298-2 |
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