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Atomistry » Magnesium » PDB 2j7k-2jg2 » 2jcb » |
Magnesium in PDB 2jcb: The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)Enzymatic activity of The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)
All present enzymatic activity of The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489):
6.3.3.2; Protein crystallography data
The structure of The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489), PDB code: 2jcb
was solved by
C.Meier,
L.G.Carter,
G.Winter,
R.J.Owens,
D.I.Stuart,
R.M.Esnouf,
Oxford Protein Production Facility (Oppf),
Structural Proteomics Ineurope (Spine),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)
(pdb code 2jcb). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489), PDB code: 2jcb: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 2jcbGo back to Magnesium Binding Sites List in 2jcb
Magnesium binding site 1 out
of 2 in the The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 2jcbGo back to Magnesium Binding Sites List in 2jcb
Magnesium binding site 2 out
of 2 in the The Crystal Structure of 5-Formyl-Tetrahydrofolate Cycloligase From Bacillus Anthracis (BA4489)
Mono view Stereo pair view
Reference:
C.Meier,
L.G.Carter,
G.Winter,
R.J.Owens,
D.I.Stuart,
R.M.Esnouf.
Structure of 5-Formyltetrahydrofolate Cyclo-Ligase From Bacillus Anthracis (BA4489). Acta Crystallogr.,Sect.F V. 63 168 2007.
Page generated: Mon Dec 14 07:29:18 2020
ISSN: ISSN 1744-3091 PubMed: 17329806 DOI: 10.1107/S1744309107007221 |
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