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Atomistry » Chlorine » PDB 5kq0-5kvy » 5ktp | |||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5kq0-5kvy » 5ktp » |
Chlorine in PDB 5ktp: Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 ClusterEnzymatic activity of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster
All present enzymatic activity of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster:
2.5.1.72; Protein crystallography data
The structure of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster, PDB code: 5ktp
was solved by
M.K.Fenwick,
S.E.Ealick,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5ktp:
The structure of Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster
(pdb code 5ktp). 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 Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster, PDB code: 5ktp: Chlorine binding site 1 out of 1 in 5ktpGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of Pyrococcus Horikoshii Quinolinate Synthase (Nada) with Bound Itaconate and FE4S4 Cluster
![]() Mono view ![]() Stereo pair view
Reference:
M.K.Fenwick,
S.E.Ealick.
Crystal Structures of the Iron-Sulfur Cluster-Dependent Quinolinate Synthase in Complex with Dihydroxyacetone Phosphate, Iminoaspartate Analogues, and Quinolinate. Biochemistry V. 55 4135 2016.
Page generated: Sat Jul 12 04:13:37 2025
ISSN: ISSN 0006-2960 PubMed: 27404889 DOI: 10.1021/ACS.BIOCHEM.6B00626 |
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