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Atomistry » Chlorine » PDB 2xsa-2xzk » 2xvx | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2xsa-2xzk » 2xvx » |
Chlorine in PDB 2xvx: Cobalt Chelatase Cbik (Periplasmatic) From Desulvobrio Vulgaris Hildenborough (Native)Enzymatic activity of Cobalt Chelatase Cbik (Periplasmatic) From Desulvobrio Vulgaris Hildenborough (Native)
All present enzymatic activity of Cobalt Chelatase Cbik (Periplasmatic) From Desulvobrio Vulgaris Hildenborough (Native):
4.99.1.3; Protein crystallography data
The structure of Cobalt Chelatase Cbik (Periplasmatic) From Desulvobrio Vulgaris Hildenborough (Native), PDB code: 2xvx
was solved by
C.V.Romao,
S.A.L.Lobo,
M.A.Carrondo,
L.M.Saraiva,
P.M.Matias,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2xvx:
The structure of Cobalt Chelatase Cbik (Periplasmatic) From Desulvobrio Vulgaris Hildenborough (Native) also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Cobalt Chelatase Cbik (Periplasmatic) From Desulvobrio Vulgaris Hildenborough (Native)
(pdb code 2xvx). 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 Cobalt Chelatase Cbik (Periplasmatic) From Desulvobrio Vulgaris Hildenborough (Native), PDB code: 2xvx: Chlorine binding site 1 out of 1 in 2xvxGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Cobalt Chelatase Cbik (Periplasmatic) From Desulvobrio Vulgaris Hildenborough (Native)
![]() Mono view ![]() Stereo pair view
Reference:
C.V.Romao,
D.Ladakis,
S.A.L.Lobo,
M.A.Carrondo,
A.A.Brindley,
E.Deery,
P.M.Matias,
R.W.Pickersgill,
L.M.Saraiva,
M.J.Warren.
Evolution in A Family of Chelatases Facilitated By the Introduction of Active Site Asymmetry and Protein Oligomerization. Proc.Natl.Acad.Sci.Usa V. 108 97 2011.
Page generated: Sat Jul 20 14:15:12 2024
ISSN: ISSN 0027-8424 PubMed: 21173279 DOI: 10.1073/PNAS.1014298108 |
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