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Atomistry » Molybdenum » PDB 4c80-5koj » 5g2s | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Molybdenum » PDB 4c80-5koj » 5g2s » |
Molybdenum in PDB 5g2s: Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with MolybdateEnzymatic activity of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate
All present enzymatic activity of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate:
2.10.1.1; Protein crystallography data
The structure of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate, PDB code: 5g2s
was solved by
J.Krausze,
C.Probst,
T.Kruse,
D.W.Heinz,
R.R.Mendel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5g2s:
The structure of Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate also contains other interesting chemical elements:
Molybdenum Binding Sites:
The binding sites of Molybdenum atom in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate
(pdb code 5g2s). This binding sites where shown within
5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate, PDB code: 5g2s: Molybdenum binding site 1 out of 1 in 5g2sGo back to![]() ![]()
Molybdenum binding site 1 out
of 1 in the Crystal Structure of the Mo-Insertase Domain CNX1E From Arabidopsis Thaliana in Complex with Molybdate
![]() Mono view ![]() Stereo pair view
Reference:
J.Krausze,
C.Probst,
U.Curth,
J.Reichelt,
S.Saha,
D.Schafflik,
D.W.Heinz,
R.R.Mendel,
T.Kruse.
Dimerization of the Plant Molybdenum Insertase CNX1E Is Required For Synthesis of the Molybdenum Cofactor. Biochem.J. V. 474 163 2017.
Page generated: Sun Aug 17 03:39:32 2025
ISSN: ISSN 0264-6021 PubMed: 27803248 DOI: 10.1042/BCJ20160846 |
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