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Atomistry » Calcium » PDB 3km6-3l4p » 3l4p | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 3km6-3l4p » 3l4p » |
Calcium in PDB 3l4p: Crystal Structure of the Aldehyde Dehydrogenase (A.K.A. Aor or Mop) of Desulfovibrio Gigas Covalently Bound to [ASO3]-Enzymatic activity of Crystal Structure of the Aldehyde Dehydrogenase (A.K.A. Aor or Mop) of Desulfovibrio Gigas Covalently Bound to [ASO3]-
All present enzymatic activity of Crystal Structure of the Aldehyde Dehydrogenase (A.K.A. Aor or Mop) of Desulfovibrio Gigas Covalently Bound to [ASO3]-:
1.2.99.7; Protein crystallography data
The structure of Crystal Structure of the Aldehyde Dehydrogenase (A.K.A. Aor or Mop) of Desulfovibrio Gigas Covalently Bound to [ASO3]-, PDB code: 3l4p
was solved by
D.R.Boer,
M.J.Romao,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3l4p:
The structure of Crystal Structure of the Aldehyde Dehydrogenase (A.K.A. Aor or Mop) of Desulfovibrio Gigas Covalently Bound to [ASO3]- also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of the Aldehyde Dehydrogenase (A.K.A. Aor or Mop) of Desulfovibrio Gigas Covalently Bound to [ASO3]-
(pdb code 3l4p). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of the Aldehyde Dehydrogenase (A.K.A. Aor or Mop) of Desulfovibrio Gigas Covalently Bound to [ASO3]-, PDB code: 3l4p: Calcium binding site 1 out of 1 in 3l4pGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Crystal Structure of the Aldehyde Dehydrogenase (A.K.A. Aor or Mop) of Desulfovibrio Gigas Covalently Bound to [ASO3]-
![]() Mono view ![]() Stereo pair view
Reference:
A.Thapper,
D.R.Boer,
C.D.Brondino,
J.J.Moura,
M.J.Romao.
Correlating Epr and X-Ray Structural Analysis of Arsenite-Inhibited Forms of Aldehyde Oxidoreductase. J.Biol.Inorg.Chem. V. 12 353 2007.
Page generated: Sat Jul 13 12:52:32 2024
ISSN: ISSN 0949-8257 PubMed: 17139522 DOI: 10.1007/S00775-006-0191-9 |
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