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Atomistry » Chlorine » PDB 4cqc-4d0m » 4csw | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4cqc-4d0m » 4csw » |
Chlorine in PDB 4csw: Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl HydroxylaseProtein crystallography data
The structure of Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase, PDB code: 4csw
was solved by
M.A.Mcdonough,
R.Sekirnik,
C.J.Schofield,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4csw:
The structure of Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase
(pdb code 4csw). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase, PDB code: 4csw: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 4cswGo back to![]() ![]()
Chlorine binding site 1 out
of 2 in the Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 2 in 4cswGo back to![]() ![]()
Chlorine binding site 2 out
of 2 in the Rhodothermus Marinus Ycfd-Like Ribosomal Protein L16 Arginyl Hydroxylase
![]() Mono view ![]() Stereo pair view
Reference:
R.Chowdhury,
R.Sekirnik,
N.C.Brissett,
T.Krojer,
C.-H.Ho,
S.S.Ng,
I.J.Clifton,
W.Ge,
N.J.Kershaw,
G.C.Fox,
J.R.C.Muniz,
M.Vollmar,
C.Phillips,
E.S.Pilka,
K.L.Kavanagh,
F.Von Deflt,
U.Oppermann,
M.A.Mcdonough,
A.J.Doherty,
C.J.Schofield.
Ribosomal Oxygenases Are Structurally Conserved From Prokaryotes to Humans. Nature V. 510 422 2014.
Page generated: Sun Jul 21 11:32:39 2024
ISSN: ISSN 0028-0836 PubMed: 24814345 DOI: 10.1038/NATURE13263 |
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