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Atomistry » Chlorine » PDB 4qgo-4qo9 » 4qnj | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4qgo-4qo9 » 4qnj » |
Chlorine in PDB 4qnj: The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A ResolutionEnzymatic activity of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution
All present enzymatic activity of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution:
4.2.1.19; Protein crystallography data
The structure of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution, PDB code: 4qnj
was solved by
C.Bisson,
K.L.Britton,
S.E.Sedelnikova,
H.F.Rodgers,
T.C.Eadsforth,
R.Viner,
T.R.Hawkes,
P.J.Baker,
D.W.Rice,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4qnj:
The structure of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution
(pdb code 4qnj). 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 The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution, PDB code: 4qnj: Chlorine binding site 1 out of 1 in 4qnjGo back to Chlorine Binding Sites List in 4qnj
Chlorine binding site 1 out
of 1 in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and Formate at 1.3A Resolution
Mono view Stereo pair view
Reference:
C.Bisson,
K.L.Britton,
S.E.Sedelnikova,
H.F.Rodgers,
T.C.Eadsforth,
R.C.Viner,
T.R.Hawkes,
P.J.Baker,
D.W.Rice.
Crystal Structures Reveal That the Reaction Mechanism of Imidazoleglycerol-Phosphate Dehydratase Is Controlled By Switching Mn(II) Coordination. Structure V. 23 1236 2015.
Page generated: Sat Dec 12 11:05:50 2020
ISSN: ISSN 0969-2126 PubMed: 26095028 DOI: 10.1016/J.STR.2015.05.012 |
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