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Atomistry » Chlorine » PDB 6gb0-6gmc » 6gkr | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 6gb0-6gmc » 6gkr » |
Chlorine in PDB 6gl6: Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377HEnzymatic activity of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H
All present enzymatic activity of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H:
1.18.99.1; Protein crystallography data
The structure of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H, PDB code: 6gl6
was solved by
L.Kertess,
T.Happe,
E.Hofmann,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6gl6:
The structure of Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H
(pdb code 6gl6). 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 Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H, PDB code: 6gl6: Chlorine binding site 1 out of 1 in 6gl6Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Apo [Fefe]-Hydrogenase HYDA1 From Chlamydomonas Reinhardtii, Variant C377H
![]() Mono view ![]() Stereo pair view
Reference:
P.Rodriguez-Macia,
L.Kertess,
J.Burnik,
J.A.Birrell,
E.Hofmann,
W.Lubitz,
T.Happe,
O.Rudiger.
His-Ligation to the [4FE-4S] Subcluster Tunes the Catalytic Bias of [Fefe] Hydrogenase. J.Am.Chem.Soc. V. 141 472 2019.
Page generated: Sat Dec 12 13:02:01 2020
ISSN: ESSN 1520-5126 PubMed: 30545220 DOI: 10.1021/JACS.8B11149 |
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