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Chlorine in PDB 4hvk: Crystal Structure and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus.Enzymatic activity of Crystal Structure and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus.
All present enzymatic activity of Crystal Structure and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus.:
2.8.1.7; Protein crystallography data
The structure of Crystal Structure and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus., PDB code: 4hvk
was solved by
Y.Yamanaka,
L.Zeppieri,
Y.Nicolet,
E.N.Marinoni,
J.S.De Oliveira,
O.Masafumi,
D.R.Dean,
J.C.Fontecilla-Camps,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4hvk:
The structure of Crystal Structure and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus. also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus.
(pdb code 4hvk). 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 and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus., PDB code: 4hvk: Chlorine binding site 1 out of 1 in 4hvkGo back to Chlorine Binding Sites List in 4hvk
Chlorine binding site 1 out
of 1 in the Crystal Structure and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus.
Mono view Stereo pair view
Reference:
Y.Yamanaka,
L.Zeppieri,
Y.Nicolet,
E.N.Marinoni,
J.S.De Oliveira,
M.Odaka,
D.R.Dean,
J.C.Fontecilla-Camps.
Crystal Structure and Functional Studies of An Unusual L-Cysteine Desulfurase From Archaeoglobus Fulgidus. Dalton Trans V. 42 3092 2013.
Page generated: Sat Dec 12 10:43:45 2020
ISSN: ISSN 1477-9226 PubMed: 23160436 DOI: 10.1039/C2DT32101G |
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