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Atomistry » Chlorine » PDB 5m86-5mge » 5mdj » |
Chlorine in PDB 5mdj: Crystal Structure of An O2-Tolerant [Nife]-Hydrogenase From Ralstonia Eutropha in A Its As-Isolated High-Pressurized FormEnzymatic activity of Crystal Structure of An O2-Tolerant [Nife]-Hydrogenase From Ralstonia Eutropha in A Its As-Isolated High-Pressurized Form
All present enzymatic activity of Crystal Structure of An O2-Tolerant [Nife]-Hydrogenase From Ralstonia Eutropha in A Its As-Isolated High-Pressurized Form:
1.12.99.6; Protein crystallography data
The structure of Crystal Structure of An O2-Tolerant [Nife]-Hydrogenase From Ralstonia Eutropha in A Its As-Isolated High-Pressurized Form, PDB code: 5mdj
was solved by
A.Schmidt,
J.Kalms,
P.Scheerer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5mdj:
The structure of Crystal Structure of An O2-Tolerant [Nife]-Hydrogenase From Ralstonia Eutropha in A Its As-Isolated High-Pressurized Form also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of An O2-Tolerant [Nife]-Hydrogenase From Ralstonia Eutropha in A Its As-Isolated High-Pressurized Form
(pdb code 5mdj). 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 Crystal Structure of An O2-Tolerant [Nife]-Hydrogenase From Ralstonia Eutropha in A Its As-Isolated High-Pressurized Form, PDB code: 5mdj: Chlorine binding site 1 out of 1 in 5mdjGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of An O2-Tolerant [Nife]-Hydrogenase From Ralstonia Eutropha in A Its As-Isolated High-Pressurized Form
![]() Mono view ![]() Stereo pair view
Reference:
J.Kalms,
A.Schmidt,
S.Frielingsdorf,
T.Utesch,
G.Gotthard,
D.Von Stetten,
P.Van Der Linden,
A.Royant,
M.A.Mroginski,
P.Carpentier,
O.Lenz,
P.Scheerer.
Tracking the Route of Molecular Oxygen in O2-Tolerant Membrane-Bound [Nife] Hydrogenase. Proc. Natl. Acad. Sci. V. 115 E2229 2018U.S.A..
Page generated: Fri Jul 26 12:36:13 2024
ISSN: ESSN 1091-6490 PubMed: 29463722 DOI: 10.1073/PNAS.1712267115 |
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