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Atomistry » Cobalt » PDB 2r5v-2xwp » 2xwp | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cobalt » PDB 2r5v-2xwp » 2xwp » |
Cobalt in PDB 2xwp: Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated TetrapyrroleEnzymatic activity of Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole
All present enzymatic activity of Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole:
4.99.1.3; Protein crystallography data
The structure of Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole, PDB code: 2xwp
was solved by
D.Ladakis,
A.A.Brindley,
E.Deery,
M.J.Warren,
R.W.Pickersgill,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole
(pdb code 2xwp). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole, PDB code: 2xwp: Cobalt binding site 1 out of 1 in 2xwpGo back to Cobalt Binding Sites List in 2xwp
Cobalt binding site 1 out
of 1 in the Anaerobic Cobalt Chelatase (Cbik) From Salmonella Typhimurium in Complex with Metalated Tetrapyrrole
Mono view Stereo pair view
Reference:
C.V.Romao,
D.Ladakis,
S.A.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: Sun Dec 13 10:39:25 2020
ISSN: ISSN 0027-8424 PubMed: 21173279 DOI: 10.1073/PNAS.1014298108 |
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